ID FIMB_YEAST Reviewed; 642 AA.
AC P32599; D6VSB5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 02-OCT-2024, entry version 211.
DE RecName: Full=Fimbrin;
DE AltName: Full=ABP67;
GN Name=SAC6; OrderedLocusNames=YDR129C; ORFNames=YD9302.04C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1956405; DOI=10.1038/354404a0;
RA Adams A.E.M., Botstein D., Drubin D.G.;
RT "Requirement of yeast fimbrin for actin organization and morphogenesis in
RT vivo.";
RL Nature 354:404-408(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867; DOI=10.1038/387s075;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds to actin, and functionally associates with actin
CC structures involved in the development and maintenance of cell
CC polarity.
CC -!- INTERACTION:
CC P32599; P60010: ACT1; NbExp=4; IntAct=EBI-6931, EBI-2169;
CC -!- MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X63867; CAA45346.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88210.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11975.1; -; Genomic_DNA.
DR PIR; S29320; S29320.
DR RefSeq; NP_010414.3; NM_001180437.3.
DR AlphaFoldDB; P32599; -.
DR SMR; P32599; -.
DR BioGRID; 32185; 315.
DR DIP; DIP-718N; -.
DR IntAct; P32599; 23.
DR MINT; P32599; -.
DR STRING; 4932.YDR129C; -.
DR iPTMnet; P32599; -.
DR PaxDb; 4932-YDR129C; -.
DR PeptideAtlas; P32599; -.
DR TopDownProteomics; P32599; -.
DR EnsemblFungi; YDR129C_mRNA; YDR129C; YDR129C.
DR GeneID; 851707; -.
DR KEGG; sce:YDR129C; -.
DR AGR; SGD:S000002536; -.
DR SGD; S000002536; SAC6.
DR VEuPathDB; FungiDB:YDR129C; -.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR HOGENOM; CLU_015284_3_0_1; -.
DR InParanoid; P32599; -.
DR OMA; WQLMRKN; -.
DR OrthoDB; 5475188at2759; -.
DR BioCyc; YEAST:G3O-29728-MONOMER; -.
DR BioGRID-ORCS; 851707; 6 hits in 10 CRISPR screens.
DR PRO; PR:P32599; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32599; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IMP:SGD.
DR CDD; cd21294; CH_FIMB_rpt1; 1.
DR CDD; cd21297; CH_FIMB_rpt2; 1.
DR CDD; cd21300; CH_FIMB_rpt3; 1.
DR CDD; cd21303; CH_FIMB_rpt4; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961:SF18; FI19014P1; 1.
DR PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 2.
DR PROSITE; PS50021; CH; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..642
FT /note="Fimbrin"
FT /id="PRO_0000073757"
FT DOMAIN 16..50
FT /note="EF-hand 1"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT DOMAIN 139..259
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 287..390
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 411..521
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 534..642
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 125..394
FT /note="Actin-binding 1"
FT REGION 395..642
FT /note="Actin-binding 2"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 71773 MW; 9AF17D056173A690 CRC64;
MNIVKLQRKF PILTQEDLFS TIEKFRAIDL DDKGWVEKQQ ALEAVSKDGD ATYDEARETL
KHVGVDASGR VELDDYVGLV AKLRESKTGA APQTTFNVAP NSTPIVSTAA TGLQHKGKGT
QAKIIVAGSQ TGTTHTINEE ERREFTKHIN SVLAGDQDIG DLLPFPTDTF QLFDECRDGL
VLSKLINDSV PDTIDTRVLN WPKKGKELNN FQASENANIV INSAKAIGCV VVNVHSEDII
EGREHLILGL IWQIIRRGLL SKIDIKLHPE LYRLLEDDET LEQFLRLPPE QILLRWFNYH
LKQANWNRRV TNFSKDVSDG ENYTILLNQL DPALCSKAPL QTTDLMERAE QVLQNAEKLD
CRKYLTPSSL VAGNPKLNLA FVAHLFNTHP GLEPIQEEEK PEIEEFDAEG EREARVFTLW
LNSLDVDPPV ISLFDDLKDG LILLQAYEKV MPGAVDFKHV NKRPASGAEI SRFKALENTN
YAVDLGRAKG FSLVGIEGSD IVDGNKLLTL GLVWQLMRRN ISITMKTLSS SGRDMSDSQI
LKWAQDQVTK GGKNSTIRSF KDQALSNAHF LLDVLNGIAP GYVDYDLVTP GNTEEERYAN
ARLAISIARK LGALIWLVPE DINEVRARLI ITFIASLMTL NK
//
