ID   CAPZA_SCHPO             Reviewed;         256 AA.
AC   Q10434;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=F-actin-capping protein subunit alpha;
GN   Name=acp1; ORFNames=SPAC12B10.07;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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 {ECO:0000269|PubMed:15743909,
CC       ECO:0000269|PubMed:16823372}. Note=Septum. Localizes to cell tips
CC       during interphase.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA94697.1; -; Genomic_DNA.
DR   PIR; T37574; T37574.
DR   RefSeq; NP_594639.1; NM_001020067.2.
DR   AlphaFoldDB; Q10434; -.
DR   SMR; Q10434; -.
DR   BioGRID; 279132; 27.
DR   MINT; Q10434; -.
DR   STRING; 4896.SPAC12B10.07.1; -.
DR   iPTMnet; Q10434; -.
DR   MaxQB; Q10434; -.
DR   PaxDb; Q10434; -.
DR   PRIDE; Q10434; -.
DR   EnsemblFungi; SPAC12B10.07.1; SPAC12B10.07.1:pep; SPAC12B10.07.
DR   GeneID; 2542679; -.
DR   KEGG; spo:SPAC12B10.07; -.
DR   PomBase; SPAC12B10.07; acp1.
DR   VEuPathDB; FungiDB:SPAC12B10.07; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; Q10434; -.
DR   OMA; HVHYYED; -.
DR   PhylomeDB; Q10434; -.
DR   Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q10434; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0008290; C:F-actin capping protein complex; 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:0030036; P:actin cytoskeleton organization; IGI:PomBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IDA:PomBase.
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; 3.30.1140.60; -; 1.
DR   Gene3D; 3.90.1150.210; -; 1.
DR   InterPro; IPR002189; CapZ_alpha.
DR   InterPro; IPR037282; CapZ_alpha/beta.
DR   InterPro; IPR042276; CapZ_alpha/beta_2.
DR   InterPro; IPR042489; CapZ_alpha_1.
DR   InterPro; IPR017865; F-actin_cap_asu_CS.
DR   PANTHER; PTHR10653; PTHR10653; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   SUPFAM; SSF90096; SSF90096; 1.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..256
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000208645"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   256 AA;  29808 MW;  2B54706CF31C9E4B CRC64;
     MEKEAIYKLI RESPPGEVNQ VVHDIRDIGL SDEEAIHEQL KLYHEDYNSS VSISDDEKVI
     ISADNRLEGN RYYDQVLQKS FTINYETMEA ENVEDYTEAI KIPDEIVKQI KKVASDHYLS
     DVTFGIIKKS DEVESFTIVL VSSKYNPKNY WNGSWRCICN YNVSEKKLEG RSHIRVHYYE
     DGNVWLDASR PISATVEETS KLYEVLAQVE NGIQQSFNVE LSSLNDKKFK ELRRQLPVTR
     QKINWENVSG IRMRNT