ID DYST_MOUSE Reviewed; 7393 AA.
AC Q91ZU6; E9PXE5; E9QL23; Q1KP04; Q3I6J6; Q60824; Q60845; Q8K5D4; Q91ZU7;
AC Q91ZU8; Q9WU50; S4R1U5;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 02-OCT-2024, entry version 195.
DE RecName: Full=Dystonin;
DE AltName: Full=Bullous pemphigoid antigen 1;
DE Short=BPA;
DE AltName: Full=Dystonia musculorum protein;
DE AltName: Full=Hemidesmosomal plaque protein;
DE AltName: Full=Microtubule actin cross-linking factor 2;
GN Name=Dst; Synonyms=Bpag1, Macf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAK83384.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Epithelium, Muscle, and Neuron;
RX PubMed=11514586; DOI=10.1083/jcb.200012098;
RA Leung C.L., Zheng M., Prater S.M., Liem R.K.H.;
RT "The BPAG1 locus: alternative splicing produces multiple isoforms with
RT distinct cytoskeletal linker domains, including predominant isoforms in
RT neurons and muscles.";
RL J. Cell Biol. 154:691-697(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=7670468; DOI=10.1038/ng0795-301;
RA Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.;
RT "The mouse dystonia musculorum gene is a neural isoform of bullous
RT pemphigoid antigen 1.";
RL Nat. Genet. 10:301-306(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING
RP (ISOFORMS 2 AND 6), AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 6).
RC STRAIN=C3H/HeJ;
RX PubMed=16289082; DOI=10.1016/j.yexcr.2005.10.002;
RA Young K.G., Pinheiro B., Kothary R.;
RT "A Bpag1 isoform involved in cytoskeletal organization surrounding the
RT nucleus.";
RL Exp. Cell Res. 312:121-134(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING
RP (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7, PALMITOYLATION,
RP MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=16797530; DOI=10.1016/j.yexcr.2006.04.025;
RA Jefferson J.J., Leung C.L., Liem R.K.;
RT "Dissecting the sequence specific functions of alternative N-terminal
RT isoforms of mouse bullous pemphigoid antigen 1.";
RL Exp. Cell Res. 312:2712-2725(2006).
RN [6]
RP PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, X-RAY CRYSTALLOGRAPHY
RP (3.0 ANGSTROMS) OF 580-803, AND SPECTRIN REPEATS.
RX PubMed=17161423; DOI=10.1016/j.jmb.2006.11.036;
RA Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.;
RT "Structural analysis of the plakin domain of bullous pemphigoid antigen1
RT (BPAG1) suggests that plakins are members of the spectrin superfamily.";
RL J. Mol. Biol. 366:244-257(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6697-7393 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6874-7393 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Fetal skin, and Fetal spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INTERACTION
RP WITH PRPH.
RC STRAIN=BALB/cJ;
RX PubMed=9971739; DOI=10.1083/jcb.144.3.435;
RA Leung C.L., Sun D., Liem R.K.;
RT "The intermediate filament protein peripherin is the specific interaction
RT partner of mouse BPAG1-n (dystonin) in neurons.";
RL J. Cell Biol. 144:435-446(1999).
RN [9]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC STRAIN=Swiss Webster / NIH;
RA Kubo Y., Ohba M., Iwashita S.;
RT "Molecular network in NGF-mediated neural differentiation.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=7736575; DOI=10.1016/0092-8674(95)90333-x;
RA Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B.,
RA Fuchs E.;
RT "Gene targeting of BPAG1: abnormalities in mechanical strength and cell
RT migration in stratified epithelia and neurologic degeneration.";
RL Cell 81:233-243(1995).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 5
RP AND 6), AND TISSUE SPECIFICITY.
RX PubMed=8752219; DOI=10.1016/s0092-8674(00)80138-5;
RA Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.;
RT "An essential cytoskeletal linker protein connecting actin microfilaments
RT to intermediate filaments.";
RL Cell 86:655-665(1996).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=10428034; DOI=10.1016/s0092-8674(00)81017-x;
RA Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.;
RT "Integrators of the cytoskeleton that stabilize microtubules.";
RL Cell 98:229-238(1999).
RN [13]
RP INTERACTION WITH DES, AND DISRUPTION PHENOTYPE.
RX PubMed=10357897; DOI=10.1006/dbio.1999.9263;
RA Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y.,
RA Leclerc N., Kothary R.;
RT "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an
RT instability of skeletal muscle cytoarchitecture.";
RL Dev. Biol. 210:367-380(1999).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING (ISOFORM 1),
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORM 1).
RX PubMed=14581450; DOI=10.1083/jcb.200306075;
RA Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C.,
RA Mobley W., Fuchs E., Yang Y.;
RT "BPAG1n4 is essential for retrograde axonal transport in sensory neurons.";
RL J. Cell Biol. 163:223-229(2003).
RN [15]
RP ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION, MUTAGENESIS
RP OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14576348; DOI=10.1242/jcs.00764;
RA Young K.G., Pool M., Kothary R.;
RT "Bpag1 localization to actin filaments and to the nucleus is regulated by
RT its N-terminus.";
RL J. Cell Sci. 116:4543-4555(2003).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [18]
RP FUNCTION, INTERACTION WITH TMEM108 (ISOFORM 1), DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17287360; DOI=10.1073/pnas.0602222104;
RA Liu J.J., Ding J., Wu C., Bhagavatula P., Cui B., Chu S., Mobley W.C.,
RA Yang Y.;
RT "Retrolinkin, a membrane protein, plays an important role in retrograde
RT axonal transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2223-2228(2007).
RN [19]
RP ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18638474; DOI=10.1016/j.yexcr.2008.06.021;
RA Young K.G., Kothary R.;
RT "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope
RT protein in sensory neurons.";
RL Exp. Cell Res. 314:2750-2761(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-237; SER-1381;
RP SER-2211; SER-4680; SER-5488; SER-7333; SER-7336 AND SER-7348,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-208 (ISOFORM 7),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC, SUBCELLULAR
RP LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
RA Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F.,
RA Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G.,
RA Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.;
RT "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle
RT and association with plectin and alpha-actinin.";
RL Exp. Cell Res. 316:297-313(2010).
RN [22]
RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR
RP LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=20209123; DOI=10.1371/journal.pone.0009465;
RA Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C.;
RT "Hearts of dystonia musculorum mice display normal morphological and
RT histological features but show signs of cardiac stress.";
RL PLoS ONE 5:E9465-E9465(2010).
CC -!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of
CC intermediate filaments, actin and microtubule cytoskeleton networks.
CC Required for anchoring either intermediate filaments to the actin
CC cytoskeleton in neural and muscle cells or keratin-containing
CC intermediate filaments to hemidesmosomes in epithelial cells. The
CC proteins may self-aggregate to form filaments or a two-dimensional
CC mesh. Regulates the organization and stability of the microtubule
CC network of sensory neurons to allow axonal transport. Mediates docking
CC of the dynein/dynactin motor complex to vesicle cargos for retrograde
CC axonal transport through its interaction with TMEM108 and DCTN1.
CC {ECO:0000269|PubMed:17287360}.
CC -!- FUNCTION: [Isoform 5]: Plays a structural role in the assembly of
CC hemidesmosomes of epithelial cells; anchors keratin-containing
CC intermediate filaments to the inner plaque of hemidesmosomes. Required
CC for the regulation of keratinocyte polarity and motility; mediates
CC integrin ITGB4 regulation of RAC1 activity.
CC -!- FUNCTION: [Isoform 6]: Required for bundling actin filaments around the
CC nucleus.
CC -!- SUBUNIT: Homodimer. Interacts with MAPRE1; probably required for
CC targeting to the growing microtubule plus ends. Isoform 2 interacts
CC (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with
CC PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with
CC COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus)
CC with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5
CC interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5
CC associates (via C-terminal) with KRT5-KRT14 (via rod region)
CC intermediate filaments of keratins (By similarity). Isoform 2 and
CC isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via
CC N-terminus) with PLEC (via N-terminus). Interacts with the neuronal
CC intermediate filament protein, PRPH. Interacts with DES. Interacts with
CC SYNE3. Isoform 1 interacts with TMEM108 (PubMed:17287360).
CC {ECO:0000250|UniProtKB:Q03001, ECO:0000269|PubMed:10357897,
CC ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:18638474,
CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:9971739}.
CC -!- INTERACTION:
CC Q91ZU6; P21807: Prph; Xeno; NbExp=3; IntAct=EBI-446159, EBI-446227;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC stress fiber. Cell projection, axon {ECO:0000269|PubMed:17287360}.
CC Note=Associates with axonal microtubules at the growing distal tip and
CC intermediate filaments, but not with actin cytoskeleton, in sensory
CC neurons (By similarity). Associates with intermediate filaments, actin
CC and microtubule cytoskeletons. Localizes to actin stress fibers and to
CC actin-rich ruffling at the cortex of cells. {ECO:0000250,
CC ECO:0000269|PubMed:14576348}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and
CC cytoplasmic actin filaments (PubMed:19932097). Localizes to vesicule-
CC like structures associated with microtubules (PubMed:14581450,
CC PubMed:17287360). {ECO:0000269|PubMed:14581450,
CC ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane, sarcolemma.
CC Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril,
CC sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to
CC microtubules and actin microfilaments throughout the cytoplasm and at
CC focal contact attachments at the plasma membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton. Cell
CC junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-KRT14
CC intermediate filaments network of keratins. Colocalizes with ITGB4 at
CC the leading edge of migrating keratinocytes (By similarity). Localizes
CC to actin and intermediate filaments cytoskeletons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus. Nucleus envelope. Membrane;
CC Single-pass membrane protein. Endoplasmic reticulum membrane; Single-
CC pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, stress fiber {ECO:0000269|PubMed:14576348}.
CC Note=Associates with actin cytoskeleton in sensory neurons (By
CC similarity). Localizes to actin and intermediate filaments
CC cytoskeletons. Localizes to central actin stress fibers around the
CC nucleus and is excluded form focal contact sites in myoblast cells.
CC Translocates to the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm, cytoskeleton. Cytoplasm,
CC cell cortex. Cell membrane; Lipid-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC Name=2 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-b, BPAG1a1,
CC dystonin-1;
CC IsoId=Q91ZU6-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-a
CC {ECO:0000303|PubMed:14581450}, BPAG1a2, BPAG1n4
CC {ECO:0000303|PubMed:14581450};
CC IsoId=Q91ZU6-2; Sequence=VSP_041549;
CC Name=3 {ECO:0000305};
CC IsoId=Q91ZU6-3; Sequence=VSP_041550, VSP_041551, VSP_041552;
CC Name=4 {ECO:0000305};
CC IsoId=Q91ZU6-4; Sequence=VSP_041551, VSP_041552;
CC Name=5; Synonyms=BPAG1-e;
CC IsoId=Q91ZU6-5; Sequence=VSP_055459, VSP_055460, VSP_055461;
CC Name=6; Synonyms=BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2;
CC IsoId=Q91ZU6-6; Sequence=VSP_041543, VSP_041546;
CC Name=7; Synonyms=BPAG1a3;
CC IsoId=Q91ZU6-8; Sequence=VSP_041542, VSP_041544, VSP_041545;
CC -!- TISSUE SPECIFICITY: Isoform 1 and 2 are expressed in striated and heart
CC muscle cells. Isoform 5 is expressed in the skin. Isoform 6 is
CC expressed in sensory neural cells of the dorsal root ganglion and with
CC low level in the skin (at protein level). Isoform 1 is expressed
CC predominantly in the brain and spinal cord with low levels in the heart
CC (PubMed:14581450). Isoform 2 is predominantly expressed in muscle and
CC heart and with low levels in the brain. Isoform 5 is expressed in the
CC skin and with low levels in myoblast cells. Isoform 6 is expressed in
CC neurons. Isoform 7 is expressed in lung and with low levels in the
CC brain. {ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:14576348,
CC ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16797530,
CC ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:19932097,
CC ECO:0000269|PubMed:20209123, ECO:0000269|PubMed:7670468,
CC ECO:0000269|PubMed:7736575, ECO:0000269|PubMed:8752219}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is the major form expressed in the
CC dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly expressed
CC in the myocardium, skeletal muscles, bone cartilage and epithelia of
CC the tongue at 14.5 dpc. Isoform 5 is expressed at high levels in the
CC epidermis and mucosal epithelia of the digestive tracts at 14.5 dpc.
CC {ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:7670468}.
CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent
CC on the tertiary structure induced by heterodimerization of these
CC intermediate filaments proteins and most likely involves recognition
CC sites located in the rod domain of these keratins.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show progressive deterioration in motor
CC function and sensory neurodegeneration. Exhibit axonal swellings packed
CC with disorganized intermediate filaments (IFs) and microtubules. Show
CC poorly defined Z lines and display a reduction in sarcomere length.
CC Have increased accumulation of vesicles and severely disrupted
CC retrograde axonal transport. In stratified epithelia, hemidesmosomes
CC are normal but they lack the inner plate and have no cytoskeleton
CC attached. {ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:10428034,
CC ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:17287360,
CC ECO:0000269|PubMed:7736575}.
CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. Transmembrane protein
CC (helical transmembrane domain from amino acid 18 to 38). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Incomplete sequence. Probably myristoylated
CC on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of
CC Gly-2 to Ala inhibits cortical localization. Mutagenesis of Cys-5 to
CC Ser inhibits cortical localization. Mutagenesis of Cys-7 to Ser
CC inhibits cortical localization. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK83382.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
CC Sequence=AAK83383.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
CC Sequence=AAK83384.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAC52231.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF396877; AAK83382.1; ALT_SEQ; mRNA.
DR EMBL; AF396878; AAK83383.1; ALT_SEQ; mRNA.
DR EMBL; AF396879; AAK83384.1; ALT_SEQ; mRNA.
DR EMBL; AC123072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U22452; AAC52230.1; -; mRNA.
DR EMBL; U25158; AAC52231.1; ALT_FRAME; mRNA.
DR EMBL; DQ023311; AAY46942.1; -; mRNA.
DR EMBL; DQ463750; ABF00406.1; -; mRNA.
DR EMBL; AK051626; BAC34695.1; -; mRNA.
DR EMBL; AK037206; BAC29753.1; -; mRNA.
DR EMBL; AF115383; AAD22959.1; -; mRNA.
DR EMBL; AB085694; BAB93448.1; -; mRNA.
DR CCDS; CCDS35534.1; -. [Q91ZU6-1]
DR CCDS; CCDS35535.1; -. [Q91ZU6-2]
DR CCDS; CCDS69875.1; -. [Q91ZU6-5]
DR PIR; A60776; A60776.
DR PIR; I49290; I49290.
DR PIR; I49298; I49298.
DR RefSeq; NP_034211.2; NM_010081.2. [Q91ZU6-5]
DR RefSeq; NP_598594.2; NM_133833.3. [Q91ZU6-2]
DR RefSeq; NP_604443.2; NM_134448.3. [Q91ZU6-1]
DR PDB; 2IAK; X-ray; 3.00 A; A=580-803.
DR PDBsum; 2IAK; -.
DR SMR; Q91ZU6; -.
DR BioGRID; 199328; 16.
DR IntAct; Q91ZU6; 9.
DR MINT; Q91ZU6; -.
DR STRING; 10090.ENSMUSP00000138308; -.
DR ChEMBL; CHEMBL2176789; -.
DR GlyGen; Q91ZU6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q91ZU6; -.
DR PhosphoSitePlus; Q91ZU6; -.
DR SwissPalm; Q91ZU6; -.
DR REPRODUCTION-2DPAGE; IPI00230689; -.
DR REPRODUCTION-2DPAGE; IPI00230690; -.
DR REPRODUCTION-2DPAGE; IPI00284272; -.
DR jPOST; Q91ZU6; -.
DR PaxDb; 10090-ENSMUSP00000095392; -.
DR PeptideAtlas; Q91ZU6; -.
DR ProteomicsDB; 279588; -. [Q91ZU6-1]
DR ProteomicsDB; 279589; -. [Q91ZU6-2]
DR ProteomicsDB; 279590; -. [Q91ZU6-3]
DR ProteomicsDB; 279591; -. [Q91ZU6-4]
DR ProteomicsDB; 279592; -. [Q91ZU6-5]
DR ProteomicsDB; 279593; -. [Q91ZU6-6]
DR ProteomicsDB; 279594; -. [Q91ZU6-8]
DR Pumba; Q91ZU6; -.
DR Antibodypedia; 31066; 197 antibodies from 23 providers.
DR DNASU; 13518; -.
DR Ensembl; ENSMUST00000097785.10; ENSMUSP00000095392.3; ENSMUSG00000026131.22. [Q91ZU6-1]
DR Ensembl; ENSMUST00000097786.10; ENSMUSP00000095393.3; ENSMUSG00000026131.22. [Q91ZU6-2]
DR Ensembl; ENSMUST00000183302.6; ENSMUSP00000138376.4; ENSMUSG00000026131.22. [Q91ZU6-5]
DR GeneID; 13518; -.
DR KEGG; mmu:13518; -.
DR UCSC; uc007aoi.2; mouse. [Q91ZU6-1]
DR UCSC; uc007aoj.2; mouse. [Q91ZU6-2]
DR UCSC; uc007aok.1; mouse. [Q91ZU6-8]
DR UCSC; uc007aol.2; mouse. [Q91ZU6-5]
DR AGR; MGI:104627; -.
DR CTD; 667; -.
DR MGI; MGI:104627; Dst.
DR VEuPathDB; HostDB:ENSMUSG00000026131; -.
DR eggNOG; KOG0516; Eukaryota.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000155008; -.
DR HOGENOM; CLU_000015_1_0_1; -.
DR InParanoid; Q91ZU6; -.
DR OMA; RQKATMV; -.
DR OrthoDB; 5489926at2759; -.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 13518; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Dst; mouse.
DR EvolutionaryTrace; Q91ZU6; -.
DR PRO; PR:Q91ZU6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91ZU6; protein.
DR Bgee; ENSMUSG00000026131; Expressed in aorta tunica media and 259 other cell types or tissues.
DR ExpressionAtlas; Q91ZU6; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0031673; C:H zone; IDA:UniProtKB.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0045098; C:type III intermediate filament; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR GO; GO:0031581; P:hemidesmosome assembly; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IDA:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd21236; CH_DYST_rpt1; 1.
DR CDD; cd21239; CH_DYST_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 15.
DR Gene3D; 1.20.58.1060; -; 1.
DR Gene3D; 1.20.58.60; -; 30.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR Gene3D; 3.90.1290.10; Plakin repeat; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR049538; PCN-like_spectrin-like_rpt.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF21; EPIPLAKIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00681; Plectin; 1.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 19.
DR Pfam; PF18373; Spectrin_2; 1.
DR Pfam; PF21019; Spectrin_3; 1.
DR Pfam; PF21020; Spectrin_4; 1.
DR Pfam; PF21097; SR_plectin_7; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00250; PLEC; 9.
DR SMART; SM00150; SPEC; 33.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR SUPFAM; SSF75399; Plakin repeat; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 26.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative promoter usage;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Intermediate filament;
KW Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule;
KW Muscle protein; Myristate; Nucleus; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Transmembrane; Ubl conjugation.
FT CHAIN 1..7393
FT /note="Dystonin"
FT /id="PRO_0000078141"
FT DOMAIN 35..138
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044,
FT ECO:0000305"
FT DOMAIN 151..255
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044,
FT ECO:0000305"
FT REPEAT 602..699
FT /note="Spectrin 1"
FT REPEAT 701..802
FT /note="Spectrin 2"
FT DOMAIN 887..944
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1292..1421
FT /note="Spectrin 3"
FT REPEAT 1439..1538
FT /note="Spectrin 4"
FT REPEAT 1584..1626
FT /note="Plectin 1"
FT REPEAT 1660..1703
FT /note="Plectin 2"
FT REPEAT 1774..1817
FT /note="Plectin 3"
FT REPEAT 1818..1855
FT /note="Plectin 4"
FT REPEAT 1856..1891
FT /note="Plectin 5"
FT REPEAT 3321..3427
FT /note="Spectrin 5"
FT REPEAT 3569..3678
FT /note="Spectrin 6"
FT REPEAT 3852..3971
FT /note="Spectrin 7"
FT REPEAT 3978..4084
FT /note="Spectrin 8"
FT REPEAT 4091..4190
FT /note="Spectrin 9"
FT REPEAT 4200..4299
FT /note="Spectrin 10"
FT REPEAT 4447..4552
FT /note="Spectrin 11"
FT REPEAT 4559..4663
FT /note="Spectrin 12"
FT REPEAT 4673..4773
FT /note="Spectrin 13"
FT REPEAT 4780..4882
FT /note="Spectrin 14"
FT REPEAT 4889..4989
FT /note="Spectrin 15"
FT REPEAT 4999..5098
FT /note="Spectrin 16"
FT REPEAT 5105..5208
FT /note="Spectrin 17"
FT REPEAT 5215..5319
FT /note="Spectrin 18"
FT REPEAT 5326..5428
FT /note="Spectrin 19"
FT REPEAT 5435..5537
FT /note="Spectrin 20"
FT REPEAT 5653..5755
FT /note="Spectrin 21"
FT REPEAT 5763..5863
FT /note="Spectrin 22"
FT REPEAT 5870..5976
FT /note="Spectrin 23"
FT REPEAT 5983..6085
FT /note="Spectrin 24"
FT REPEAT 6092..6195
FT /note="Spectrin 25"
FT REPEAT 6202..6304
FT /note="Spectrin 26"
FT REPEAT 6311..6413
FT /note="Spectrin 27"
FT REPEAT 6420..6522
FT /note="Spectrin 28"
FT REPEAT 6529..6632
FT /note="Spectrin 29"
FT REPEAT 6639..6740
FT /note="Spectrin 30"
FT REPEAT 6747..6849
FT /note="Spectrin 31"
FT REPEAT 6859..6989
FT /note="Spectrin 32"
FT DOMAIN 7019..7054
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7055..7090
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7095..7173
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 35..252
FT /note="Actin-binding"
FT REGION 2114..2200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2216..2253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2274..2425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2473..2820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3044..3063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3281..3317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7180..7199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7217..7275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7303..7393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1382..1388
FT /note="Nuclear localization signal; in isoform 6"
FT MOTIF 7373..7376
FT /note="Microtubule tip localization signal"
FT COMPBIAS 2114..2142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2321..2343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2384..2425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2479..2499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2505..2539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2540..2558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2560..2576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2620..2636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2677..2693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2763..2780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2791..2805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3049..3063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3295..3309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7183..7199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7233..7251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7338..7352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7370..7384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7032
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7034
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7036
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7038
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7043
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7068
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7070
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7072
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7074
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7079
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03001"
FT MOD_RES 3894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03001"
FT MOD_RES 4680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03001"
FT MOD_RES 7333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 5401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03001"
FT VAR_SEQ 1..381
FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV
FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV
FT NIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAG
FT VRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD
FT PEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIR
FT HHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEKSKIKRLYKLLEIWIEFGRI
FT KLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVE -> MQSSSYSYRSSDSVFSNTTST
FT RTSLDSNENLLSVHCGPTLINSCISFSNESLDGH (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11514586"
FT /id="VSP_055459"
FT VAR_SEQ 1..137
FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV
FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV
FT NIRNDDITDGNPKLTLGLIWTIILHF -> MGNVCGCVRAEKEEPYFDPAKSPLSPEKY
FT SPGRKYFRRKPCQKVVDDTEPVRQSSEREGKKGVSQPAGGQPAVSSGELPWEDPAASPT
FT KEDAVQLGKRAATEHGDQKPLPSSVDGYPHRVTVSSAQGRYSEVQVSIPDKIISEEDSP
FT PYCPETERHLDDVNSKHRTFLRKDNVSLSQTAASSSPILCVTEKSLKNSALMGNLSRSC
FT HSVLEQDSDERGHPFGVHRLQLTKRRCHSLSSGVSCVSKDAPRDDGC (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:16797530"
FT /id="VSP_041542"
FT VAR_SEQ 1..30
FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYK -> MIAAAFLVLLRPYSIQCA
FT LFLLLLLLGTVATIVFFCCWHRKLQKGRHPMKSVFSGRSRSRDAALRSHHFRSEGFRAS
FT PRHIRRRVAAAAAARLEEVKPVVEVHHQSEQESSGRKRRIKKNSRVQPEFYHSVQGAST
FT RRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASPAPGDTLPWNLPKHERSKRKIQGGS
FT VLDPAERAVLRIA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16289082"
FT /id="VSP_041543"
FT VAR_SEQ 271..272
FT /note="VK -> KG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16797530"
FT /id="VSP_041544"
FT VAR_SEQ 273..7393
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16797530"
FT /id="VSP_041545"
FT VAR_SEQ 305..7393
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16289082"
FT /id="VSP_041546"
FT VAR_SEQ 1432
FT /note="K -> MKRSKENSEHGAYSDLLQRQRATMVENSKLTGKISELETMVAELKKQ
FT KSRVEEELPKVKEAAENELRKQQRNVEDIALQKLRAESEAKQYRRELETIVREKEAAER
FT ELERVRQLTAEAEARRAAVEENLRNFRSQLQENTFTRQTLEDHLRRKDSSLSDLEQQKR
FT ALVEELQRKRDHEEELLRLVKQMERDLAFQKQVAEKQLKEKQKVELEARRKITEIQFSC
FT RESAAVAQARPQREQGRQKEEELKQQVDELTLANRKAEKEMRELKYELSAVQLEKASSE
FT EKARLLKDKLDETNNTLKCLKEDLERKDQAQERYSQQLRDLGRQLNQTTDKAEEVRQEA
FT NDLKKIKHTYQLELESLHQEKGKLQREVDRVTRAHALAERNIQCLNSQVHASRDEKDLS
FT EERRRLCQRKSDHLKEEFERSHAQLLQNIQAEKENNDKIQKLNKELEKSNECAETLKQK
FT VDELTRQNNETKLMMQRIQAESKNIVREKQAIQQRCEVLRIQADGFKDQLRNTNEHLHK
FT QTKTEQDFHRKIKSLEDDLAQSQNLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKE
FT EKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSAD
FT EFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYR
FT EKMQQGPPVEANHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQCEIQKK
FT STTQDHTFASAFDTAGRECHHPAEISPGNSGHLNLKTRLPLSRWTQEPHQTEGKWPHRA
FT AEQLPKEVQFRQPGAPLDRESSQPCYSEYFSQTSTELQITFDDKNPITRLSELETMREQ
FT ALHPSRPPVTYQDDKLERELVKLLTPLEIAKNKQCGMHTEVTTLKQEKRLGSSAGGWML
FT EGCRTSGGLKGDFLKKSVEPEASPSLDLNQACSVRDEEFQFQGLRHTVTGRQLVEAKLL
FT DMRTVEQLRLGLKTVEEVQRSLSKFLTKATSIAGLYLESSKEKMSFTSAAQKIIIDKMI
FT ALAFLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGYSHASKTL
FT SVFQAMENRMLDRKKGKHILEAQIASGGVIDPVRGVRVPPEMAVQQGLLNNAVLQFLHE
FT PSSNTRVFPNPNNKQALYYSELLQICVFDVDCQCFLLPFGEREISNLNIEKTHKIAVVD
FT TKTGAELTAFEAFQRNLIDKGIYLELSGQQYQWKEATFFDSYGHPSHMLTDTKTGLQFN
FT ISEAVEQGTLDKALVQKYQEGLTTLTELADFLLSKVVPKKDLHSPIAGYWLTASGERIS
FT LLKASRRNLVDRVTALRCLEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFAQQLRQC
FT ELVITGISHPVSNKMMSVVEAVNANIISKEMGMRCLEFQYLTGGLIEPKVFSRLTIEEA
FT LHVGIIDVLIATRLKDQKSYVRDIMCPQTKRKLTYKEALEKADFDFHTGLKLLEVSEPL
FT GTGISNLYYSSQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11514586"
FT /id="VSP_055460"
FT VAR_SEQ 1433..7393
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11514586"
FT /id="VSP_055461"
FT VAR_SEQ 1549..3562
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11514586"
FT /id="VSP_041549"
FT VAR_SEQ 7129..7134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041550"
FT VAR_SEQ 7174..7197
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041551"
FT VAR_SEQ 7265
FT /note="K -> KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041552"
FT MUTAGEN 1385
FT /note="R->A: Prevents isoform 6 from localizing to the
FT nucleus; when associated with A-1386."
FT /evidence="ECO:0000269|PubMed:14576348"
FT MUTAGEN 1386
FT /note="R->A: Prevents isoform 6 from localizing to the
FT nucleus; when associated with A-1385."
FT /evidence="ECO:0000269|PubMed:14576348"
FT HELIX 590..593
FT /evidence="ECO:0007829|PDB:2IAK"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 608..623
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 631..650
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 652..661
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:2IAK"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 670..686
FT /evidence="ECO:0007829|PDB:2IAK"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 690..722
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 744..767
FT /evidence="ECO:0007829|PDB:2IAK"
FT HELIX 773..793
FT /evidence="ECO:0007829|PDB:2IAK"
FT CONFLICT Q91ZU6-6:101
FT /note="E -> K (in Ref. 3; AAC52231)"
FT /evidence="ECO:0000305"
FT MOD_RES Q91ZU6-8:205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q91ZU6-8:208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 7393 AA; 834218 MW; C3CDF88978C33EF1 CRC64;
MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK
EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC
SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS
SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI
SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE
SEVAYDWSER NSSVARKKSY HAELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR
AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI
HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI
EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF ANRIEQQYQS
VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE
DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES
CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP
SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK
EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP
ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK
SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ
HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT
TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR
QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL
QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP
QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI
WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN
TASVLKSVTL PDKMPDLGDL EDCKNAKRWL SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS
SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV
LTIPDAFPDC ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN
GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL KGCKSQSEPV
TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF DYSPRLSALL SHDELRQSQG
RFSDTSTPQN TGYLCEASTL SPSDQRVLAD QSTREKFQDQ FLGIAAISVS LQGAPCGQKP
VDTECSSSQV HYHSEESMSD ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS
DCGPLSHKGA IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD
CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN KVCCPQGFPV
GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE SDSLTEGEII GRKERLGASL
TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ SSESYRPYMS DGSDLDEEDN GGRSSEDSGD
GRGGQGVADE GGEPQYQADP TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG
VFQPESAGRG GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ
GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD RDQQGPGRGL
VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER DLEPFPNGSA TESLNMGKSQ
VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG EAKNVQTGLT ESPVLLETLA EIFDTPASKV
TRADLTSAVT ASEMKSQVKE DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL
VAPPTVKDNL CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD
STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE KASAEEEPHR
ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV GDPSAGTGTK ISIQNLIRRA
ILSELPNEVS NVPSHGISPI SNSSEVRAES GGDPFCITSF LHLLKQNQPP QETPGISELA
KVLTQMDCDP EQRGLGSELL PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK
PHVCSDLRNK EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS
KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS LEALKSQLKQ
LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE LSKSHQRLQN AFSSLSSVSS
ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS YSDWVSEKSR SVKAIQTVNV QDTELVKNSV
KFLKNVLADL SHTKMQLETT AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL
VTTEADRLEA LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD
GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA LIEQKLNEVK
MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE SKTKIENLLN WLSNVEEDSE
GVWTKHTQPM EQNGTYLHEG DSKLGAGEED EVNGNLLETD AEGHSEATKG NLNQQYEKVK
AQHGKIMAQH QAVLLATQSA QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK
VKLTHSLQEE LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI
SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD QVTDRFRSLY
SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK HLREPIALDP KNLQRQLEET
KALQGQISSQ QVAVEKLKKT AEVLLDAKGS LLPAKNDIQK TLDDIVGRYD DLSKCVNERN
EKLQITLTRS LSVQDALDEM LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG
RQSSINAMNE KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE
QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD LEALHSLLKE
ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS CQEQLSAFQT LAQSLKTWIK
ETTKQVPVVK PSLGTEDLRK SLEETKKLQE KWNLKAPEIH KANNSGVSLC NLLSALISPA
KAIAAAKSGG VILNGEGTDT NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN
TKLSKLQKAQ EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV
NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK LEESSNNLTQ
FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ ILLQEFDTRK PQYEQLTAAG
QGILSRPGED PSLHGIVNEQ LEAVTQKWDN LTGQLRDRCD WIDQAIVKST QYQSLLRSLS
GTLTELDDKL SSGLTSGALP DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE
EYLKAELSRQ LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ
RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG AEKAALQLQL
NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP WIDRCQHSLD GVTFSLDPTE
SESSIAELKS LQKEMDHHFG MLELLNNTAN SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ
LQSKTVSLEN MAQKFKEFQE VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK
SLQTLKQQVD EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK
LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK KLEALMASND
SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA KTREEQVDGA TEKLEEFHRK
LEEFSTLLQK AEEHEESQGP VGTETETINQ QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL
IQSAAANTCT QGLEHDLDSV NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA
DTEELVANQK PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV
KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA VEKKLANSEP
IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL KQTTGDEVLI IQDKLEAIKA
RYKDITKLSA DVAKTLEHAL QLAGQLQSMH KELCNWLDKV EVELLSYETQ GLKGEAASQV
QERQKELKNE VRSNKALVDS LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ
KVEEIDAAIL RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI
LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER HLQLERAQSL
VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE EHRQLRELIA EHKPHIDKMN
KTGPQLLELS PKEGIYIQEK YVAADTLYSQ IKEDVKKRAV VLDEAISQST QFHDKIDQIL
ESLERIAERL RQPPSISAEV EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG
TEKDVSARAV QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ
DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA CGEPDKPIVK
KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG IFDWVDIAGN KLATMSPIGT
DLETVKQQIE ELKQFKSEAY QQQIEMERLN HQAELLLKKV TEEADKHTVQ DPLMELKLIW
DSLDERIVSR QHKLEGALLA LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA
KHHVLQNDVL AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK
QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA HMEVCTAFAI
KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES VKSKLNEKKT KLEEALHLAM
NFHNSLQDFI NWLTQAEQTL NVASRPSLIL DTILFQIDEH KVFANEVNSH REQIIELDKT
GTHLKYFSQK QDVVLIKNLL ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME
WLEESEKSLD SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA
DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID WLYRVEPQLA
EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA RELIEGSRDD SSWVRVQMQE
LSTRWETVCA LSISKQTRLE SALQQAEEFH SVVHTLLEWL AEAEQTLRFH GALPDDEDAL
RTLIEQHKEF MKRLEEKRAE LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW
AKQHQQRLAG ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT
FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG FYPSGSQTQI
ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE FANFDFDIWR KKYMRWMNHK
KSRVMDFFRR IDKDQDGKIT RQEFIDGILS SKFPTSRLEM SAVADIFDRD GDGYIDYYEF
VAALHPNKDA YKPITDADKI EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ
LRLVRILRST VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG
RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC QAASPPVPAA
ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR VRTQFAESRK TPSRPGSRAG
SKAGSRASSR RGSDASDFDI SEIQSVCSDV ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR
RSPASKLDKS SKR
//
