ID   CAPZA_CANGA             Reviewed;         262 AA.
AC   Q6FN48;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=F-actin-capping protein subunit alpha;
GN   Name=CAP1; OrderedLocusNames=CAGL0K02783g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; CR380957; CAG61307.1; -; Genomic_DNA.
DR   RefSeq; XP_448346.1; XM_448346.1.
DR   AlphaFoldDB; Q6FN48; -.
DR   SMR; Q6FN48; -.
DR   STRING; 5478.XP_448346.1; -.
DR   EnsemblFungi; CAG61307; CAG61307; CAGL0K02783g.
DR   GeneID; 2890272; -.
DR   KEGG; cgr:CAGL0K02783g; -.
DR   CGD; CAL0134955; CAGL0K02783g.
DR   VEuPathDB; FungiDB:CAGL0K02783g; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; Q6FN48; -.
DR   OMA; HVHYYED; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:EnsemblFungi.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   Actin capping; Actin-binding; Reference proteome.
FT   CHAIN           1..262
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000208642"
SQ   SEQUENCE   262 AA;  29667 MW;  670D4DE63D4FFFD6 CRC64;
     MSNDFDTIIK NIIKDSPAGE LEEVYQDLIT IAGENSKETI IDAIAEYNVE NSIPIDVDGK
     DVIISKYNKQ GTKFVDPVNG IQFSVDHLHQ KGLDVEEYSA DIDADQKKAI TDLGNYLSTN
     FPGRATFAVL PLEEQSKTAI IIVSTKYNPS NFWNGHWKSE YVYDKTEGKL SGTIDIDVHY
     YEDGNVKFHS SKLVEETNIK DPVASIKELE HKFEQDLQES FTDLNEKQFK SLRRRLPITR
     ARVNWGKAIG NYRLGRDAAQ GK