CAPZB_YEAST
ID CAPZB_YEAST Reviewed; 287 AA.
AC P13517; D6VVP8; Q07082;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=F-actin-capping protein subunit beta;
GN Name=CAP2; OrderedLocusNames=YIL034C;
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=2179733; DOI=10.1038/344352a0;
RA Amatruda J.F., Cannon J.F., Tatchell K., Hug C., Cooper J.A.;
RT "Disruption of the actin cytoskeleton in yeast capping protein mutants.";
RL Nature 344:352-354(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA Amatruda J.F., Gattermeir D.J., Cooper J.A.;
RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-195.
RX PubMed=2823100; DOI=10.1128/mcb.7.8.2653-2663.1987;
RA Cannon J.F., Tatchell K.;
RT "Characterization of Saccharomyces cerevisiae genes encoding subunits of
RT cyclic AMP-dependent protein kinase.";
RL Mol. Cell. Biol. 7:2653-2663(1987).
RN [6]
RP PROTEIN SEQUENCE OF 149-156, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1315784; DOI=10.1083/jcb.117.5.1067;
RA Amatruda J.F., Cooper J.A.;
RT "Purification, characterization, and immunofluorescence localization of
RT Saccharomyces cerevisiae capping protein.";
RL J. Cell Biol. 117:1067-1076(1992).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. {ECO:0000269|PubMed:1315784}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:1315784}.
CC -!- INTERACTION:
CC P13517; P28495: CAP1; NbExp=5; IntAct=EBI-4013, EBI-4003;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:1315784}. Bud {ECO:0000269|PubMed:1315784}. Bud tip
CC {ECO:0000269|PubMed:1315784}. Note=Found at cortical actin spots at the
CC site of bud emergence and at the tips of growing buds and shmoos.
CC -!- MISCELLANEOUS: Present with 6770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; X62630; CAA44497.1; -; Genomic_DNA.
DR EMBL; Z46861; CAA86917.1; -; Genomic_DNA.
DR EMBL; M17223; AAA66935.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08514.1; -; Genomic_DNA.
DR PIR; S49944; S49944.
DR RefSeq; NP_012230.3; NM_001179384.3.
DR AlphaFoldDB; P13517; -.
DR SMR; P13517; -.
DR BioGRID; 34956; 211.
DR ComplexPortal; CPX-1637; F-actin capping protein complex.
DR DIP; DIP-836N; -.
DR IntAct; P13517; 13.
DR MINT; P13517; -.
DR STRING; 4932.YIL034C; -.
DR iPTMnet; P13517; -.
DR MaxQB; P13517; -.
DR PaxDb; P13517; -.
DR PRIDE; P13517; -.
DR EnsemblFungi; YIL034C_mRNA; YIL034C; YIL034C.
DR GeneID; 854777; -.
DR KEGG; sce:YIL034C; -.
DR SGD; S000001296; CAP2.
DR VEuPathDB; FungiDB:YIL034C; -.
DR eggNOG; KOG3174; Eukaryota.
DR GeneTree; ENSGT00390000017957; -.
DR HOGENOM; CLU_045864_1_1_1; -.
DR InParanoid; P13517; -.
DR OMA; MIEDMEI; -.
DR BioCyc; YEAST:G3O-31306-MON; -.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P13517; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P13517; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:ComplexPortal.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0008290; C:F-actin capping protein complex; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA: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; IMP:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:SGD.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR Gene3D; 1.20.58.570; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR001698; CAPZB.
DR InterPro; IPR043175; CAPZB_N.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..287
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000204642"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 140
FT /note="F -> Y (in Ref. 5; AAA66935)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="FK -> I (in Ref. 5; AAA66935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 32629 MW; 6E669023D1378778 CRC64;
MSDAQFDAAL DLLRRLNPTT LQENLNNLIE LQPNLAQDLL SSVDVPLSTQ KDSADSNREY
LCCDYNRDID SFRSPWSNTY YPELSPKDLQ DSPFPSAPLR KLEILANDSF DVYRDLYYEG
GISSVYLWDL NEEDFNGHDF AGVVLFKKNQ SDHSNWDSIH VFEVTTSPSS PDSFNYRVTT
TIILHLDKTK TDQNSHMMLS GNLTRQTEKD IAIDMSRPLD VIFTSHVANL GSLIEDIESQ
MRNLLETVYF EKTRDIFHQT KNAAIASSAE EANKDAQAEV IRGLQSL
