ID SYNE1_MOUSE Reviewed; 8799 AA.
AC Q6ZWR6; Q8K3T7; Q9ERT7; Q9ERT8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 02-OCT-2024, entry version 155.
DE RecName: Full=Nesprin-1 {ECO:0000305};
DE AltName: Full=Enaptin;
DE AltName: Full=KASH domain-containing protein 1;
DE Short=KASH1;
DE AltName: Full=Myocyte nuclear envelope protein 1;
DE Short=Myne-1;
DE AltName: Full=Nuclear envelope spectrin repeat protein 1;
DE AltName: Full=Synaptic nuclear envelope protein 1;
DE Short=Syne-1;
GN Name=Syne1 {ECO:0000312|MGI:MGI:1927152};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 6808-8799 (ISOFORM 4), INTERACTION WITH MUSK, AND SUBCELLULAR LOCATION.
RX PubMed=10878022; DOI=10.1074/jbc.m004775200;
RA Apel E.D., Lewis R.M., Grady R.M., Sanes J.R.;
RT "Syne-1, a dystrophin- and Klarsicht-related protein associated with
RT synaptic nuclei at the neuromuscular junction.";
RL J. Biol. Chem. 275:31986-31995(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, ACTIN-BINDING,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15093733; DOI=10.1016/j.yexcr.2004.01.014;
RA Padmakumar V.C., Abraham S., Braune S., Noegel A.A., Tunggal B.,
RA Karakesisoglou I., Korenbaum E.;
RT "Enaptin, a giant actin-binding protein, is an element of the nuclear
RT membrane and the actin cytoskeleton.";
RL Exp. Cell Res. 295:330-339(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Vagina;
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12958361; DOI=10.1126/science.1088176;
RA Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.;
RT "Nuclear membrane proteins with potential disease links found by
RT subtractive proteomics.";
RL Science 301:1380-1382(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8308, AND IDENTIFICATION BY
RP 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 [7]
RP FUNCTION.
RX PubMed=19596800; DOI=10.1242/jcs.043794;
RA Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A.,
RA Gull K., Johnson C.A.;
RT "Nesprin-2 interacts with meckelin and mediates ciliogenesis via
RT remodelling of the actin cytoskeleton.";
RL J. Cell Sci. 122:2716-2726(2009).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19874786; DOI=10.1016/j.neuron.2009.08.018;
RA Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.;
RT "SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus
RT during neurogenesis and neuronal migration in mice.";
RL Neuron 64:173-187(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19509342; DOI=10.1073/pnas.0812037106;
RA Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y.,
RA Xu R., Han M.;
RT "SUN1 and SUN2 play critical but partially redundant roles in anchoring
RT nuclei in skeletal muscle cells in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732; THR-2268; SER-5655;
RP THR-8278; SER-8284 AND THR-8363, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-377 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-8225 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and 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 [11]
RP SELF-ASSOCIATION, INTERACTION WITH SYNE3, AND TISSUE SPECIFICITY.
RX PubMed=22518138; DOI=10.1155/2012/736524;
RA Taranum S., Sur I., Muller R., Lu W., Rashmi R.N., Munck M., Neumann S.,
RA Karakesisoglou I., Noegel A.A.;
RT "Cytoskeletal interactions at the nuclear envelope mediated by nesprins.";
RL Int. J. Cell Biol. 2012:736524-736524(2012).
RN [12]
RP INTERACTION WITH SPAG4.
RX PubMed=26621829; DOI=10.1242/bio.015768;
RA Pasch E., Link J., Beck C., Scheuerle S., Alsheimer M.;
RT "The LINC complex component Sun4 plays a crucial role in sperm head
RT formation and fertility.";
RL Biol. Open 4:1792-1802(2015).
CC -!- FUNCTION: Multi-isomeric modular protein which forms a linking network
CC between organelles and the actin cytoskeleton to maintain the
CC subcellular spatial organization. As a component of the LINC (LInker of
CC Nucleoskeleton and Cytoskeleton) complex involved in the connection
CC between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic
CC interactions established by the LINC complex play an important role in
CC the transmission of mechanical forces across the nuclear envelope and
CC in nuclear movement and positioning. May be involved in nucleus-
CC centrosome attachment. During interkinetic nuclear migration (INM) at
CC G2 phase and nuclear migration in neural progenitors its LINC complex
CC association with SUN1/2 and probably association with cytoplasmic
CC dynein-dynactin motor complexes functions to pull the nucleus toward
CC the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum,
CC midbrain, brain stem, and other brain regions except cerebral cortex
CC and hippocampus. Required for centrosome migration to the apical cell
CC surface during early ciliogenesis. May be involved in nuclear
CC remodeling during sperm head formation in spermatogenesis; a probable
CC SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior
CC cytoskeletal structures such as the manchette.
CC {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:19596800,
CC ECO:0000269|PubMed:19874786}.
CC -!- SUBUNIT: Core component of LINC complexes which are composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC containing proteins seem to bind each other promiscuously; however,
CC differentially expression of LINC complex constituents can give rise to
CC specific assemblies. At least SUN1/2-containing core LINC complexes are
CC proposed to be hexameric composed of three protomers of each KASH and
CC SUN domain-containing protein. The SUN2:SYNE1/KASH1 LINC complex is a
CC heterohexamer; the homotrimeric cloverleave-like conformation of the
CC SUN domain is a prerequisite for LINC complex formation in which three
CC separate SYNE1/KASH1 peptides bind at the interface of adjacent SUN
CC domains. Self-associates. Interacts with SYNE3. Interacts with SUN3;
CC proposed to form a spermatogenesis-specific LINC complex with SUN3
CC during sperm head formation. May interact with MUSK. Interacts with
CC SPAG4/SUN4. Interacts with EMD and LMNA in vitro. Interacts with F-
CC actin via its N-terminal domain. Interacts with DCTN1 and DYNC1I1/2;
CC suggesting the association with the dynein-dynactin motor complex.
CC Interacts (via KASH domain) with TMEM258 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:10878022,
CC ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:22518138,
CC ECO:0000269|PubMed:26621829}.
CC -!- INTERACTION:
CC Q6ZWR6-5; Q6ZWR6-5: Syne1; NbExp=2; IntAct=EBI-10760805, EBI-10760805;
CC Q6ZWR6-5; Q6ZMZ3-1: SYNE3; Xeno; NbExp=2; IntAct=EBI-10760805, EBI-10760907;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000305}; Single-pass
CC type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm,
CC myofibril, sarcomere {ECO:0000250}. Note=The largest part of the
CC protein is cytoplasmic, while its C-terminal part is associated with
CC the nuclear envelope, most probably the outer nuclear membrane. In
CC skeletal and smooth muscles, a significant amount is found in the
CC sarcomeres (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Nesprin-1 Giant, Enaptin;
CC IsoId=Q6ZWR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZWR6-2; Sequence=VSP_038791, VSP_038796, VSP_038797,
CC VSP_038798;
CC Name=3; Synonyms=Syne-1A;
CC IsoId=Q6ZWR6-3; Sequence=VSP_038791, VSP_038796, VSP_038797;
CC Name=4; Synonyms=Syne-1B;
CC IsoId=Q6ZWR6-4; Sequence=VSP_038797;
CC Name=5; Synonyms=Enaptin-165;
CC IsoId=Q6ZWR6-5; Sequence=VSP_038792, VSP_038793, VSP_038794,
CC VSP_038795;
CC -!- TISSUE SPECIFICITY: Expressed in C2F3 and CH310T1/2 cells, brain and
CC skeletal muscle (at protein level). {ECO:0000269|PubMed:15093733,
CC ECO:0000269|PubMed:22518138}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to SUN1 and SUN2 through recognition of their SUN domains.
CC {ECO:0000250}.
CC -!- PTM: The disulfid bond with SUN1 or SUN2 is required for stability of
CC the respective LINC complex under tensile forces.
CC {ECO:0000250|UniProtKB:Q8WXH0}.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG24393.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF281869; AAG24392.1; -; mRNA.
DR EMBL; AF281870; AAG24393.1; ALT_FRAME; mRNA.
DR EMBL; AF535143; AAN03487.1; -; mRNA.
DR EMBL; AK036828; BAC29595.1; -; mRNA.
DR EMBL; AC156392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56679.1; -. [Q6ZWR6-3]
DR CCDS; CCDS56680.1; -. [Q6ZWR6-5]
DR RefSeq; NP_001073154.1; NM_001079686.1.
DR SMR; Q6ZWR6; -.
DR BioGRID; 211015; 13.
DR DIP; DIP-60966N; -.
DR IntAct; Q6ZWR6; 10.
DR MINT; Q6ZWR6; -.
DR STRING; 10090.ENSMUSP00000039440; -.
DR CarbonylDB; Q6ZWR6; -.
DR GlyConnect; 2530; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q6ZWR6; 1 site, 1 glycan.
DR GlyGen; Q6ZWR6; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites).
DR iPTMnet; Q6ZWR6; -.
DR PhosphoSitePlus; Q6ZWR6; -.
DR jPOST; Q6ZWR6; -.
DR PaxDb; 10090-ENSMUSP00000039440; -.
DR PeptideAtlas; Q6ZWR6; -.
DR ProteomicsDB; 254843; -. [Q6ZWR6-1]
DR ProteomicsDB; 254844; -. [Q6ZWR6-2]
DR ProteomicsDB; 254845; -. [Q6ZWR6-3]
DR ProteomicsDB; 254846; -. [Q6ZWR6-4]
DR ProteomicsDB; 254847; -. [Q6ZWR6-5]
DR Pumba; Q6ZWR6; -.
DR Antibodypedia; 19931; 198 antibodies from 27 providers.
DR DNASU; 64009; -.
DR Ensembl; ENSMUST00000041639.7; ENSMUSP00000039440.6; ENSMUSG00000096054.4. [Q6ZWR6-5]
DR Ensembl; ENSMUST00000095899.5; ENSMUSP00000093587.4; ENSMUSG00000096054.4. [Q6ZWR6-3]
DR GeneID; 64009; -.
DR KEGG; mmu:64009; -.
DR UCSC; uc007egn.1; mouse. [Q6ZWR6-5]
DR UCSC; uc007egt.2; mouse. [Q6ZWR6-2]
DR AGR; MGI:1927152; -.
DR CTD; 23345; -.
DR MGI; MGI:1927152; Syne1.
DR VEuPathDB; HostDB:ENSMUSG00000096054; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154481; -.
DR HOGENOM; CLU_000034_0_1_1; -.
DR InParanoid; Q6ZWR6; -.
DR OrthoDB; 5478539at2759; -.
DR PhylomeDB; Q6ZWR6; -.
DR TreeFam; TF317709; -.
DR TreeFam; TF337116; -.
DR BioGRID-ORCS; 64009; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Syne1; mouse.
DR PRO; PR:Q6ZWR6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6ZWR6; protein.
DR Bgee; ENSMUSG00000096054; Expressed in cerebellar cortex and 222 other cell types or tissues.
DR ExpressionAtlas; Q6ZWR6; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd21241; CH_SYNE1_rpt1; 1.
DR CDD; cd21243; CH_SYNE1_rpt2; 1.
DR CDD; cd00176; SPEC; 10.
DR Gene3D; 1.20.58.60; -; 31.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR039906; Anc-1/SYNE1/2-like.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR047290; CH_SYNE1_rpt1.
DR InterPro; IPR047291; CH_SYNE1_rpt2.
DR InterPro; IPR012315; KASH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR21524:SF5; KLARSICHT PROTEIN; 1.
DR PANTHER; PTHR21524; SPECTRIN REPEAT CONTAINING NUCLEAR ENVELOPE PROTEIN 2; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF10541; KASH; 1.
DR Pfam; PF00435; Spectrin; 11.
DR SMART; SM00033; CH; 2.
DR SMART; SM01249; KASH; 1.
DR SMART; SM00150; SPEC; 42.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 48.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS51049; KASH; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Disulfide bond; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..8799
FT /note="Nesprin-1"
FT /id="PRO_0000392209"
FT TOPO_DOM 1..8748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TRANSMEM 8749..8769
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 8770..8799
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT DOMAIN 27..134
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 178..283
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 314..397
FT /note="Spectrin 1"
FT REPEAT 398..502
FT /note="Spectrin 2"
FT REPEAT 503..609
FT /note="Spectrin 3"
FT REPEAT 610..703
FT /note="Spectrin 4"
FT REPEAT 704..815
FT /note="Spectrin 5"
FT REPEAT 816..923
FT /note="Spectrin 6"
FT REPEAT 924..1024
FT /note="Spectrin 7"
FT REPEAT 1025..1122
FT /note="Spectrin 8"
FT REPEAT 1123..1246
FT /note="Spectrin 9"
FT REPEAT 1247..1333
FT /note="Spectrin 10"
FT REPEAT 1334..1442
FT /note="Spectrin 11"
FT REPEAT 1443..1548
FT /note="Spectrin 12"
FT REPEAT 1549..1651
FT /note="Spectrin 13"
FT REPEAT 1652..1761
FT /note="Spectrin 14"
FT REPEAT 1762..1877
FT /note="Spectrin 15"
FT REPEAT 1878..1974
FT /note="Spectrin 16"
FT REPEAT 1975..2079
FT /note="Spectrin 17"
FT REPEAT 2080..2193
FT /note="Spectrin 18"
FT REPEAT 2194..2301
FT /note="Spectrin 19"
FT REPEAT 2302..2399
FT /note="Spectrin 20"
FT REPEAT 2400..2511
FT /note="Spectrin 21"
FT REPEAT 2512..2617
FT /note="Spectrin 22"
FT REPEAT 2618..2729
FT /note="Spectrin 23"
FT REPEAT 2730..2836
FT /note="Spectrin 24"
FT REPEAT 2837..2960
FT /note="Spectrin 25"
FT REPEAT 2961..3060
FT /note="Spectrin 26"
FT REPEAT 3061..3169
FT /note="Spectrin 27"
FT REPEAT 3170..3273
FT /note="Spectrin 28"
FT REPEAT 3274..3385
FT /note="Spectrin 29"
FT REPEAT 3386..3488
FT /note="Spectrin 30"
FT REPEAT 3489..3591
FT /note="Spectrin 31"
FT REPEAT 3592..3718
FT /note="Spectrin 32"
FT REPEAT 3719..3812
FT /note="Spectrin 33"
FT REPEAT 3813..3918
FT /note="Spectrin 34"
FT REPEAT 3919..4026
FT /note="Spectrin 35"
FT REPEAT 4027..4137
FT /note="Spectrin 36"
FT REPEAT 4138..4233
FT /note="Spectrin 37"
FT REPEAT 4234..4337
FT /note="Spectrin 38"
FT REPEAT 4338..4449
FT /note="Spectrin 39"
FT REPEAT 4450..4558
FT /note="Spectrin 40"
FT REPEAT 4559..4667
FT /note="Spectrin 41"
FT REPEAT 4668..4774
FT /note="Spectrin 42"
FT REPEAT 4775..4880
FT /note="Spectrin 43"
FT REPEAT 4881..4989
FT /note="Spectrin 44"
FT REPEAT 4990..5097
FT /note="Spectrin 45"
FT REPEAT 5098..5207
FT /note="Spectrin 46"
FT REPEAT 5208..5316
FT /note="Spectrin 47"
FT REPEAT 5317..5422
FT /note="Spectrin 48"
FT REPEAT 5423..5520
FT /note="Spectrin 49"
FT REPEAT 5521..5628
FT /note="Spectrin 50"
FT REPEAT 5629..5745
FT /note="Spectrin 51"
FT REPEAT 5746..5851
FT /note="Spectrin 52"
FT REPEAT 5971..6080
FT /note="Spectrin 53"
FT REPEAT 6081..6187
FT /note="Spectrin 54"
FT REPEAT 6377..6488
FT /note="Spectrin 55"
FT REPEAT 6489..6584
FT /note="Spectrin 56"
FT REPEAT 6585..6694
FT /note="Spectrin 57"
FT REPEAT 6695..6798
FT /note="Spectrin 58"
FT REPEAT 6799..6905
FT /note="Spectrin 59"
FT REPEAT 6906..7023
FT /note="Spectrin 60"
FT REPEAT 7024..7131
FT /note="Spectrin 61"
FT REPEAT 7132..7240
FT /note="Spectrin 62"
FT REPEAT 7241..7353
FT /note="Spectrin 63"
FT REPEAT 7354..7457
FT /note="Spectrin 64"
FT REPEAT 7458..7561
FT /note="Spectrin 65"
FT REPEAT 7562..7674
FT /note="Spectrin 66"
FT REPEAT 7675..7786
FT /note="Spectrin 67"
FT REPEAT 7787..7886
FT /note="Spectrin 68"
FT REPEAT 7887..8000
FT /note="Spectrin 69"
FT REPEAT 8001..8109
FT /note="Spectrin 70"
FT REPEAT 8110..8221
FT /note="Spectrin 71"
FT REPEAT 8332..8440
FT /note="Spectrin 72"
FT REPEAT 8441..8550
FT /note="Spectrin 73"
FT REPEAT 8551..8668
FT /note="Spectrin 74"
FT DOMAIN 8740..8799
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REGION 1..289
FT /note="Actin-binding"
FT REGION 1288..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5868..5894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 8237..8287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 8673..8735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..8666
FT /evidence="ECO:0000255"
FT COMPBIAS 5871..5894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8251..8271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8673..8722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 8227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NF91"
FT MOD_RES 8278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 8281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NF91"
FT MOD_RES 8284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 8308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 8363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 8776
FT /note="Interchain (with C-577 in SUN2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT DISULFID 8776
FT /note="Interchain (with C-759 in SUN1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT VAR_SEQ 1..7828
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10878022,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038791"
FT VAR_SEQ 103
FT /note="K -> KSMYRGSP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15093733"
FT /id="VSP_038792"
FT VAR_SEQ 297..313
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15093733"
FT /id="VSP_038793"
FT VAR_SEQ 1435..1441
FT /note="DIKTMEM -> EYVLHHF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15093733"
FT /id="VSP_038794"
FT VAR_SEQ 1442..8799
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15093733"
FT /id="VSP_038795"
FT VAR_SEQ 7829..7878
FT /note="IAVAQENKIQLQEMGERLAKASHESKASEIQYKLSRVKDRWQHLLDLMAA
FT -> MVVAEDLHGPRMAEDSSVDADLPDCDCDVS (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10878022,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038796"
FT VAR_SEQ 8218..8219
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10878022,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038797"
FT VAR_SEQ 8328
FT /note="S -> SDVVIPENPEAYVKLTENAIRNTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038798"
FT CONFLICT 1086
FT /note="G -> W (in Ref. 2; AAN03487)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="I -> T (in Ref. 2; AAN03487)"
FT /evidence="ECO:0000305"
FT CONFLICT 7187
FT /note="E -> G (in Ref. 1; AAG24393)"
FT /evidence="ECO:0000305"
FT CONFLICT 7876
FT /note="M -> I (in Ref. 1; AAG24393)"
FT /evidence="ECO:0000305"
FT CONFLICT 8266
FT /note="P -> L (in Ref. 1; AAG24392/AAG24393)"
FT /evidence="ECO:0000305"
FT MOD_RES Q6ZWR6-2:377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q6ZWR6-3:377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q6ZWR6-4:8225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 8799 AA; 1009926 MW; 2A457DC081969CF0 CRC64;
MATSRASSRS HRDITNVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV DDLFEDMKDG
IKLLALLEVL SGQKLPCEQG HRVKRIHAVA NIGTALKFLE GRKIKLVNIN ATDIADGRPS
IVLGLMWTII LYFQIEELTS NLPQLQSLSS SASSVDSMVS TETASPPSKR KVAAKIQGNA
KKTLLKWVQH TAGKQMGIEV KDFGKSWRTG LAFHSVIHAI QPELVDLEKV KTRSNRENLE
DAFTIAETQL GIPRLLDPED VDVDKPDEKS IMTYVAQFLT QYPDIHGAGC DGQEDDVVFV
GFTNNIALLL GFQRDDRLIL KETKVWIEQF ERDFTRAQMT ESSLQDKYQA FKHFRVQYEM
KRKQVEHIIQ PLQRDGKLTL DQALVKQCWE RVSSRLFDWH IQLDKSLPAP LGTIGAWLYR
AEVALREEIT IQQVHEETAN TIQRKLEQHK DLLQNTDAHK RAFHEIYQTR SVNGIPMPPD
QLEDMAERFH FVSSTSELHL MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVELLL
QSYISFIENS KFFEQYEVTY QILKQTADIY VKAEGSVEEA ENVMKFMSEA TAQWRNLSVE
VRSVRSMLEE VISNWDRYGD TVASLQAWLE DAEKMLSQSE HAKKDFFRNL PHWIQQHTAM
NDAGNFLIET CDEIVSRDLK QQLLLLNGRW RELFMEVKQY ARADEMDRMK KEYIDVTTTL
FGFATEAHRK LSEPLEVSFI NVKLLIQDLE DLEKRVPVMD AQYKMIAKKA HLFAKESPQE
EANEMLTTMS KLKEQLSKVK ECCSPLLYEA QQLTVPLEEL ETQITSFYDS LGKINEILSV
LEQEAQSSTL FKQKHQELLA SQENCKKSLT LIEKGSQSVQ KLVTSSQARK PWDHTKLQKQ
IADVHHAFQS MIKKTGDWKK HVEANSRLMK KFEESRAELE KVLRVAQEGL EEKGDPEELL
RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA VRKLHKQWKD LQGEAPYHLL
HLKIAVEKDR FSAAVEECRA ELEQETKLAP QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL
IEELCGKLPV QDPVRDTCGA CHTALKELKA SIDNTYTMLV DDPDKWKDYT SRFSEFSSWV
SAKKACLKKI KDEPIDTGNH DEVKHMVDEI RNDITKKGES LSWLKSRLKY LIDISSENEA
QKRGDELAEL SSSFKALVAL LSEVEKLLSN FGECVQYKEI VKSSLEGLIS GPQESKEEAE
MILDSKNLLE AQQLLLHHQQ KTKMISAKKR DLQEQMEQAQ QGGQAGPGQE ELRKLESTLT
GLEQSRERQE RRIQVSLRKW ERFETNKETV VRYLFQTGSS HERFLSFSSL ESLSSELEQT
KEFSKRTESI ATQAENLVKE AAELPLGPRN KRVLQRQAKS IKEQVTTLED TLEEDIKTME
MVKSKWDHFG SNFETLSIWI LEKENELSSL EASASAADVQ ISQIKVTIQE IESKIDSIVG
LEEEAQSFAQ FVTTGESARI KAKLTQIRRY WEELQEHARG LEGTILGHLS QQQKFEENLR
KIRQSVSEFA ERLADPIKIC SSAAETYKVL QEHMDLCQAV ESLSSTVTMF SASAQKAVNR
ESCTQEAAAL QQQYEEILHK AKEMQTALED LLARWQRLEK GLSPFLTWLE RCEAIASSPE
KDISADRGKV ESELQLIQAL QNEVVSQASL YSNLLQLKEA LFSVASKEDV AVMKLQLEQL
DERWGDLPQI ISKRMHFLQS VLAEHKQFDE LLFSFSVWIK QFLGELQRTS EINLRDHQVA
LTRHKDHAAE IEKKRGEITH LQGHLSQLRS LGRAQDLHPL QSKVDDCFQL FEEASQVVER
RKLALAQLAE FLQSHACMST LLYQLRQTVE ATKSMSKKQS DSLKTDLHSA IQDVKTLESS
AISLDGTLTK AQCHLKSASP EERTSCRATT DQLSLEVERI QNLLGTKQSE ADALVALKEA
FREQKEELLR SIEDIEERMD RERLKVPTRQ ALQHRLRVFN QLEDELNSHE HELCWLKDKA
KQIAQKDVAF APEVDREING LEATWDDTRR QIHENQGQCC GLIDLVREYQ SLKSTVCNVL
EDASNVVVMR ATIKDQGDLK WAFSKHETSR NEMNSKQKEL DSFTSKGKHL LSELKKIHSG
DFSLVKTDME STLDKWLDVS ERIEENMDML RVSLSIWDDV LSRKDEIEGW SNSSLPKLAE
NISNLNNSLR AEELLKELES EVKIKALKLE DLHSKINNLK ELTKNPETPT ELQFIEADLR
QKLEHAKEIT EEARGTLKDF TAQRTQVERF VKDITAWLIN VEESLTRCAQ TETCEGLKKA
KDIRKELQSQ QNSITSTQEE LNSLCRKHHS VELESLGRAM TGLIKKHEAT SQLCSQTQAR
IQDSLEKHFS GSMKEFQEWF LGAKAAARES SNLTGDSQIL EARLHNLQGV LDSLSDGQSK
LDVVTQEGQT LYAHLPKQIV SSIQEQITKA NEEFQAFLKQ CLKEKQALQD CVSELGSFED
QHRKLNLWIH EMEERLKTEN LGESKHHISE KKNEVRKVEM FLGELLAARE SLDKLSQRGQ
LLSEESHSAG KGGCRSTQLL TSYQSLLRVT KEKLRSCQLA LKEHEALEEA TQSMWARVKD
VQDRLACAES TLGNKETLEG RLSQIQDILL MKGEGEVKLN LAIGKGDQAL RSSNKEGQQA
IQDQLEMLKK AWAEAMNSAV HAQSTLESVI DQWNDYLEKK SQLEQWMESV DQRLEHPLQL
QPGLKEKFSL LDHFQSIVSE AEDHTGALQQ LAAKSRELYQ KTQDESFKEA GQEELRTQFQ
DIMTVAKEKM RTVEDLVKDH LMYLDAVQEF ADWLHSAKEE LHRWSDTSGD PSATQKKLLK
IKELIDSREI GAGRLSRVES LAPAVKQNTA ASGCELLNSE MQALRADWRQ WEDCLFQTQS
SLESLVSEMA LSEQEFFGQV TQLEQALEQF CTLLKTWAQQ LTLLEGKNSD EEILECWHKG
REILDALQKA EPMTEDLKSQ LNELCRFSRD LSPYSEKVSG LIKEYNCLCL QASKGCQNKE
QILQERFQKA SRGFQQWLVN AKITTAKCFD LPQNLSEVSS SLQKIQEFLS ESENGQHKLN
TMLFKGELLS SLLTEEKAQA VQAKVLTAKE EWKSFHANLH QKESALENLK IQMKDFEVSA
ELVQNWLSKT ERLVQESSNR LYDLPAKRRE QQKLQSVLEE IQCYEPQLHR LKEKARQLWE
GQAASKSFVH RVSQLSSQYL ALSNVTKEKV SRLDRIIAEH NRFSQGVKEL QDWMSDAVHM
LDSYCLPTSD KSVLDSRMLK LEALLSVRQE KEIQMKMVVT RGEYVLQSTS LEGSAAVQQQ
LQAVKDMWES LLSAAIRCKS QLEGALSKWT SYQDDVRQFS SWMDSVEVSL TESEKQHTEL
REKITALGKA KLLNEEVLSH SSLLETIEVK RAAMTEHYVT QLELQDLQER HQALKEKAKE
AVTKLEKLVR LHQEYQRDLK AFESWLEQEQ EKLDRCSVHE GDTNAHETML RDLQELQVRC
AEGQALLNSV LHTREDVIPS GLPQAEDRVL ESLRQDWQVY QHRLAEARMQ LNNVVNKLRL
MEQKFQQADE WLKRMEEKIN FRSECQSSRS DKEIQLLQLK KWHEDLSAHR DEVEEVGTRA
QGILDETHIS SRMGCQATQL TSRYQALLLQ VLEQIKFFEE ELQCLEETES SLSSYSDWYG
STHKNFKNVA TKIDKVDESM MGKKLKTLEV LLKDMEKGHS LLKSAREKGE RAMKFLAEHE
AEALRKEIHT YMEQLKNLTS TVRKECMSLE KGLHLAKEFS DKYKVLAQWM AEYQEILCTP
EEPKMELYEK KAQLSKYKSL QQMVLSHEPS VTSVQEKSEA LLELVQDQSL KDKIQKLQSD
FQDLCSRAKE RVFSLEAKVK DHEDYNTELQ EVEKWLLQMS GRLVAPDLLE MSSLETITQQ
LAHHKAMMEE IAGFEDRLDN LKAKGDTLIG QCPEHLQAKQ KQTVQAHLQG TKDSYSAICS
TAQRVYRSLE YELQKHVSSQ DTLQQCQAWI SAVQPDLKPS PQPPLSRAEA VKQVKHFRAL
QEQARTYLDL LCSMCDLSNS SVKNTAKDIQ QTEQLIEQRL VQAQNLTQGW EEIKSLKAEL
WIYLQDADQQ LQNMKRRHTE LEINIAQNMV MQVKDFIKQL QCKQVSVSTI VEKVDKLTKN
QESPEHKEIT HLNDQWQDLC LQSDKLCAQR EQDLQRTSSY HDHMRVVEAF LEKFTTEWDS
LARSNAESTA IHLEALKKLA LALQEEMYAI DDLKDCKQKL IEQLGLDDRE LVREQTSHLE
QRWFQLQDLV KRKIQVSVTN LEELNVIQSR FQELMEWAEE QQPNIVEALK QSPPPGMAQH
LLMDHLAICS ELEAKQVLLK SLMKDADRVM ADLGLNERKV IQKALSEAQK HVSCLSDLVG
QRRKYLNKAL SEKTQFLMAV FQATSQIQQH ERKIVFREYI CLLPDDVSKQ VKTCKTAQAS
LKTYQNEVTG LCAQGRELMK GITKQEQEEV LGKLQELQTV YDTVLQKCSH RLQELEKSLV
SRKHFKEDFD KACHWLKQAD IVTFPEINLM NEKTELHAQL DKYQSILEQS PEYENLLLTL
QTTGQAMLPS LNEVDHSYLS EKLSALPQQF NVIVALAKDK FYKTQEAILA RKEYTSLIEL
TTQSLGDLED QFLKMRKMPS DLIVEESVSL QQSCSALLGE VVALGEAVNE LNQKKESFRS
TGQPWQPEKM LQLATLYHRL KRQAEQRVSF LEDTTSVYKE HAQMCRQLES QLEVVKREQA
KVNEETLPAE EKLKVYHSLA GSLQDSGILL KRVATHLEDL SPHLDPTAYE KAKSQVQSWQ
EELKQMTSDV GELVTECESR MVQSIDFQTE MSRSLDWLRR VKAELSGPVC LDLSLQDIQE
EIRKIQIHQE EVLSSLRIMS ALSHKEQEKF TKAKELISAD LEHTLAELQE LDGDVQEALR
TRQATLTEIY SRCQRYYQVF QAANDWLDDA QEMLQLAGNG LDVESAEENL RSHMEFFKTE
GQFHSNMEEL RGLVARLDPL IKATGKEELA QKMASLEKRS QGIIQESHTQ RDLLQRCMVQ
WQEYQKAREG VIELMNDAEK KLSEFAVLKT SSIHEAEEKL SKHKALVSVV DSFHEKIVAL
EEKASQLEQT GNDTSKATLS RSMTTVWQRW TRLRAVAQDQ EKILEDAVDE WKRLSAKVKE
TTEVINQLQG RLPGSSTEKA SKAELMTLLE SHDTYLMDLE SQQLTLGVLQ QRALSMLQDR
AFPGTEEEVP ILRAITALQD QCLNMQEKVK NHGKLVKQEL QEREAVETRI NSVKSWVQET
KDYLGNPTIE IDTQLEELKR LLAEATSHQE SIEKIAEEQK NKYLGLYTVL PSEISLQLAE
VALDLKIHDQ IQEKVQEIEE GKAMSQEFSC KIQKVTKDLT TILTKLKAKT DDLVHAKAEH
KMLGEELDGC NSKLMELDAA IQTFSERHSQ LGQPLAKKIG KLTELHQQTI RQAENRLSKL
NQALSHMEEY NEMLETVRKW IEKAKVLVHG NIAWNSASQL QEQYILHQTL LEESGEIDSD
LEAMAEKVQH LANVYCTGKL SQQVTQFGRE MEELRQAIRV RLRNLQDAAK DMKKFEGELR
NLQVALEQAQ TILTSPEVGR RSLKEQLCHR QHLLSEMESL KPKMQAVQLC QSALRIPEDV
VASLPLCHAA LRLQEEASQL QHTAIQQCNI MQAKKHSLIF PPKEAVVQYE QYKQEMKHLQ
QLIEEAHREI EDKPVATSNI QELQAQISLH EELAQKIKGY QEQIDSLNSK CKMLTMKAKH
ATMLLTVTEV EGLAEGTEDL DRELHPTPSA HPSVVMMTAG RCHTLLSPVT EESGEEGTNS
EISSPPACRS PSPVANTEAA VNQDIAYYQA LSAEGLQTDA ARIPPSAAVS QELYEPGLEP
SATAKLGDLQ RSWETLKNVI SEKQRTLYEV LERQQKYQDS LQSISTKMEA MEMKLGESLE
PSRSPESQMA EHQALMDEVQ MLQDEINGLQ VSLAEELVAE SQESDPAEQL ALQSTLTVLA
ERMSTIRMKA AGKRQLLEEK LSDQLEEQRQ EQALQRYRCE ADELDHWLLN TKATLDVALG
TSQEPMDMDA QLVDCQNMLV EIEQKVVALS QLSVHNENLL LEGKAHTKEE AEQLAVKLRL
LKGSLGELQR ALHDRQLDMQ GVTQEKEEND VDFTDTQSPG VQEWLAQART TRTHQRQSSL
QQQKEFEQEL AEQKSLLRSV ASRGEEILTQ HSTAEGSGGL GEKPDVLSQE LGIAEDQMRV
KWESLHQEFS AKQKLLQNIL EQEQEQVLYS SPNRLLSGVL PFRGEAQTQD KTSVTSLLDG
LSQAFGEASS QSGGTDRQSI HLEQKLYDGV SATSTWLNDV EERLFVATAP LPEETEACLF
NQEALAKDIK EMSEEMDKNK NLFSQAFPED SDNRDVIEDT LGCLLGRLSL LDSVVDQRCH
QMKERLQQIL RFQNDLKVLF TSLADSKYII LQKLANVFEQ PIVEQMQAIQ QAEEGLRDLE
GGISELKRWA DKLQVEQSAV QELSKLQDMY DELLMTVSSR RSSLHQNLAL KSQYDKALQD
LVDLLDTGQE KMTGDQKIIV CSKEEIQQLL GKHKEYFQGL ESHMILTEIL FRKIVGFAAV
KETQFHTDCM AQASAVLKQA HKRGVELEYI LEMWSHLDEN RQELSRQLEV IENSIPSVGL
VEESEDRLVE RTNLYQHLKS SLNEYQPKLY QALDDGKRLL MSVSCSELES QLNQLGEHWL
SNTNKVSKEL HRLETILKHW TRYQSEAAAL NHWLQCAKDR LAFWTQQSVT VPQELEMVRD
HLSAFLEFSK EVDAKSALKS SVTSTGNQLL RLKKVDTAAL RAELSRMDSQ WTDLLTGIPV
VQEKLHQLQM DKLPSRHAIS EVMSWISLME SVILKDEEDI RNAIGYKAIH EYLQKYKGFK
IDLNCKQLTA DFVNQSVLQI SSQDVESKRS DKTDFAEQLG AMNKSWQLLQ GRVGEKIQML
EGLLESWSEY ENSVQSLKAW FANQERKLKE QHLLGDRNSV ENALKDCQEL EDLIKAKEKE
VEKIEQNGLA LIQNKREEVS GSVMSTLQEL RQTWISLDRT VEQLKIQLTS ALGQWSNHKA
ACDEINGHLM EARYSLSRFR LLTGSSEAVQ VQVDNLQNLH DELEKQEGGL QKFGSITNQL
LKECHPPVAE TLSSTLQEVN MRWNNLLEEI AEQLHSSKAL LQLWQRYKDY SKQCASAIQR
QEEQTSVLLK AATNKDIADD EVTKWIQDCN DLLKGLETVK DSLFILRELG EQLGQQVDVS
AAAAIQCEQL CFSQRLGALE QALCKQQAVL QAGVVDYETF AKSLEALEVW MVEAEGILQG
QDPTHSSDLS TIQERMEELK GQMLKFSSLA PDLDRLNELG YRLPLNDKEI KRMQNLNRHW
SLTSSQTTER FSKLQSFLLQ HQTFLEKCET WMEFLVQTEH KLAVEISGNY QHLLEQQRAH
ELFQAEMFSR QQILHSIIVD GQNLLEQGQV DDREEFSLKL TLLSNQWQGV IRRAQQRRGI
IDSQIRQWQR YREMAEKLRK WLAEVSHLPL SGLGNIPVPL QQVRMLFDEV QFKEKVFLRQ
QGSYILTVEA GKQLLLSADS GAEAALQAEL TDIQEKWKAA SMHLEEQKKK LAFLLKDWEK
CERGIANSLE KLRMFKKRLS QPLPDHHEEL HAEQMRCKEL ENAVGRWTDD LTELMLVRDA
LAVYLSAEDI SMLKERVELL QRQWEELCHQ VSLRRQQVSE RLNEWAVFSE KNKELCEWLT
QMESKVSQNG DILIEEMIEK LKKDYQEEIA VAQENKIQLQ EMGERLAKAS HESKASEIQY
KLSRVKDRWQ HLLDLMAARV KKLKETLVAV QQLDKNMGSL RTWLAHMESE LAKPIVYDSC
NSEEIQRKLN EQQELQRDIE KHSTGVASVL NLCEVLLHDC DACATDAECD SIQQATRNLD
RRWRNICAMS MERRLKIEET WRLWQKFLDD YSRFEDWLEV SERTAAFPSS SGVLYTVAKE
ELKKFEAFQR QVHESLTQLE LINKQYRRLA RENRTDSACS LRQMVHGGNQ RWDDLQKRVT
SILRRLKHFI SQREEFETAR DSILVWLTEM DLQLTNIEHF SECDVQAKIK QLKAFQQEIS
LNHNKIEQII AQGEQLIEKS EPLDAAVIEE ELDELRRYCQ EVFGRVERYH KKLIRLPVRL
PDDHDLSDRE LDLEDSTALS DLRWQDPSAD GMPSPQPSSN PSLSLPQPLR SERSGRDTPA
SVDSIPLEWD HDYDLSRDLE SASRTLPSED EEGEEDKEFY LRGAVGLSGD PSSLESQMRQ
LDKALDDSRF QIQQTANILR SKTPTGPDLD TSYKGYMKLL GECSGSIDSV RRLEHKLAEE
ESFPGFVNLN STETQTAGVI DRWELLQAQA MSKELRMKQN LQKWQQFNSD LNNIWAWLGE
TEEELDRLQH LALSTDIHTI ESHIKKLKEL QKAVDHRKAI ILSINLCSSE FTQADSKESH
DLQDRLSQMN GRWDRVCSLL EDWRGLLQDA LMQCQEFHEM SHALLLMLEN IDRRKNEIVP
IDSTLDPETL QDHHKQLMQI KQELLKSQLR VASLQDMSRQ LLVNAEGSDC LEAKEKVHVI
GNRLKLLLKE VSHHIKDLEK LLDMSSSQQD LSSWSSADEL DTSGSVSPTS GRSTPNRQKS
PRGKCSLSQP GPSVSSPKSR STRDGSDSSR SDPRPERVGR AFLFRILRAA LPFQLLLLLL
IGLTCLVPMS EKDYSCALSN NFARSFHPML RYTNGPPPL
//
