ID   CAPZB_SCHPO             Reviewed;         268 AA.
AC   Q9HGP5;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=F-actin-capping protein subunit beta;
GN   Name=acp2; ORFNames=SPAC631.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=15743909; DOI=10.1091/mbc.e04-09-0781;
RA   Kovar D.R., Wu J.-Q., Pollard T.D.;
RT   "Profilin-mediated competition between capping protein and formin Cdc12p
RT   during cytokinesis in fission yeast.";
RL   Mol. Biol. Cell 16:2313-2324(2005).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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. Competes with formin cdc12 for attachment to the actin
CC       filaments barbed ends. Slowly replaces cdc12 on the barbed ends in
CC       preparation for filament disassembly during contractile ring
CC       constriction. {ECO:0000269|PubMed:15743909}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000269|PubMed:15743909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15743909}. Nucleus {ECO:0000269|PubMed:16823372}.
CC       Note=Septum. Localizes to cell tips during interphase.
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAC05483.1; -; Genomic_DNA.
DR   RefSeq; NP_593619.3; NM_001019050.3.
DR   AlphaFoldDB; Q9HGP5; -.
DR   SMR; Q9HGP5; -.
DR   BioGRID; 279812; 44.
DR   STRING; 4896.SPAC631.01c.1; -.
DR   iPTMnet; Q9HGP5; -.
DR   MaxQB; Q9HGP5; -.
DR   PaxDb; Q9HGP5; -.
DR   PRIDE; Q9HGP5; -.
DR   EnsemblFungi; SPAC631.01c.1; SPAC631.01c.1:pep; SPAC631.01c.
DR   GeneID; 2543390; -.
DR   KEGG; spo:SPAC631.01c; -.
DR   PomBase; SPAC631.01c; acp2.
DR   VEuPathDB; FungiDB:SPAC631.01c; -.
DR   eggNOG; KOG3174; Eukaryota.
DR   HOGENOM; CLU_045864_1_1_1; -.
DR   InParanoid; Q9HGP5; -.
DR   OMA; MIEDMEI; -.
DR   PhylomeDB; Q9HGP5; -.
DR   Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR   Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q9HGP5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0099079; C:actin body; IDA:PomBase.
DR   GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0008290; C:F-actin capping protein complex; IDA:PomBase.
DR   GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR   GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR   GO; GO:0044396; P:actin cortical patch organization; IMP:PomBase.
DR   GO; GO:1904600; P:actin fusion focus assembly; IMP:PomBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IDA:PomBase.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IGI:PomBase.
DR   GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR   GO; GO:0110055; P:negative regulation of actin filament annealing; IDA:PomBase.
DR   GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IDA:PomBase.
DR   GO; GO:0090339; P:negative regulation of formin-nucleated actin cable assembly; IMP:PomBase.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
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   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..268
FT                   /note="F-actin-capping protein subunit beta"
FT                   /id="PRO_0000204641"
SQ   SEQUENCE   268 AA;  29845 MW;  7E781ADB7B275BEE CRC64;
     MNSEDAALDL LRRLNPKDIS KNLDTILSVA PDLADVLLSS VDQPLKVNTC SESGNQYLLC
     DFNRDGDSYR SPWSNKYDPP LEDGLVSTDR VRKLEVSLNE AIRVYLDLYY EGGVSSVYLW
     DQDDSYAGAV LIKKASTSNS SGWDSIHVFE CLPTTETNVY DYRLTSTIIL FLSSGSEEQS
     ALPSKALNLS GHLTRQTSQR LPAADDDTEI ANVGKLVEEM ETRMRNFLQD VYFGKTKDII
     NQTRSIQPVS DAQPNDSALR SVLNDLSI