ID   CAPZA_YARLI             Reviewed;         262 AA.
AC   Q6C6Y4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=F-actin-capping protein subunit alpha;
GN   Name=CAP1; OrderedLocusNames=YALI0E05291g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79159.2; -; Genomic_DNA.
DR   RefSeq; XP_503578.2; XM_503578.2.
DR   AlphaFoldDB; Q6C6Y4; -.
DR   SMR; Q6C6Y4; -.
DR   STRING; 4952.CAG79159; -.
DR   EnsemblFungi; CAG79159; CAG79159; YALI0_E05291g.
DR   GeneID; 2912288; -.
DR   KEGG; yli:YALI0E05291g; -.
DR   VEuPathDB; FungiDB:YALI0_E05291g; -.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; Q6C6Y4; -.
DR   OMA; LKVDVHY; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
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; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..262
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000255620"
SQ   SEQUENCE   262 AA;  28699 MW;  1669C5222CB715DC CRC64;
     MSRSNQEALA DFVADAPPGE LNQVVEAIST VVDGNSSILS KLETDVHNKI LDQCMVVSLG
     KSKSLVSKYN QLSKDTFYDS QSGQKFEFDF DTKKATPSGS HGSDSPIQGA LDKYFSAHFP
     SEGAAGVFPQ DDGSIALVLV DGKYNPANYW NGKWRSVYIF ESGSLSGTID VDVHYYEDGN
     VRLKSSEKVD LGSVSESDIV DAISKAEQQF QEKLNKSFNG LNEDSFKALR RQLPVTRSKI
     NWGKSISNYR LGKDINVGGG RE