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   27-MAR-2024, entry version 217.
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; 214.
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; 4932-YIL034C; -.
DR   PeptideAtlas; P13517; -.
DR   EnsemblFungi; YIL034C_mRNA; YIL034C; YIL034C.
DR   GeneID; 854777; -.
DR   KEGG; sce:YIL034C; -.
DR   AGR; SGD:S000001296; -.
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; GRTTHYK; -.
DR   OrthoDB; 118970at2759; -.
DR   BioCyc; YEAST:G3O-31306-MONOMER; -.
DR   Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR   Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 854777; 5 hits in 10 CRISPR screens.
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; F-actin capping protein, beta subunit; 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; F-ACTIN-CAPPING PROTEIN SUBUNIT BETA; 1.
DR   PANTHER; PTHR10619:SF0; F-ACTIN-CAPPING PROTEIN SUBUNIT BETA; 1.
DR   Pfam; PF01115; F_actin_cap_B; 1.
DR   PRINTS; PR00192; FACTINCAPB.
DR   SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 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
//