ID   CAPZA_DEBHA             Reviewed;         266 AA.
AC   Q6BNP4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=F-actin-capping protein subunit alpha;
GN   Name=CAP1; OrderedLocusNames=DEHA2E20020g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Note=Septum. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; CR382137; CAG88449.2; -; Genomic_DNA.
DR   RefSeq; XP_460176.2; XM_460176.1.
DR   AlphaFoldDB; Q6BNP4; -.
DR   SMR; Q6BNP4; -.
DR   STRING; 4959.XP_460176.2; -.
DR   EnsemblFungi; CAG88449; CAG88449; DEHA2E20020g.
DR   GeneID; 2902750; -.
DR   KEGG; dha:DEHA2E20020g; -.
DR   VEuPathDB; FungiDB:DEHA2E20020g; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; Q6BNP4; -.
DR   OMA; HVHYYED; -.
DR   OrthoDB; 1200844at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
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; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   3: Inferred from homology;
KW   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..266
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000255617"
SQ   SEQUENCE   266 AA;  30009 MW;  9C82AAF291D2EB1B CRC64;
     MSSSVGLDTI VSSLVKSSPP GELDGISQDL SAILSSKSNS STVNTAIEKY INENSGVFSS
     TYIASKINKH ESSTKYIDFI GKKLFNIDLH KQTAIDFEDY EPEVKYPAYF DELVKKLTEY
     GEDHYPSKYA FTIVPDGSDL QIIIIGQKLN YENFYTGLWK SHYKIKSGSI EGEAKLDIHY
     YEDGNVRLNF EESTSGTLSS SNASEIVNFI NNAENEMTLK IVEDFNELNQ KYFKNLRRLL
     PVTRSKINWG QAIGNYRLGS DVVHNK