ID   CAPZA_ASHGO             Reviewed;         261 AA.
AC   Q75DS4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-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=ABR007C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50777.1; -; Genomic_DNA.
DR   RefSeq; NP_982953.1; NM_208306.1.
DR   AlphaFoldDB; Q75DS4; -.
DR   SMR; Q75DS4; -.
DR   STRING; 33169.AAS50777; -.
DR   EnsemblFungi; AAS50777; AAS50777; AGOS_ABR007C.
DR   GeneID; 4619045; -.
DR   KEGG; ago:AGOS_ABR007C; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; Q75DS4; -.
DR   OMA; HVHYYED; -.
DR   Proteomes; UP000000591; Chromosome II.
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.
PE   3: Inferred from homology;
KW   Actin capping; Actin-binding; Reference proteome.
FT   CHAIN           1..261
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000208641"
SQ   SEQUENCE   261 AA;  29684 MW;  D709E80952D1F352 CRC64;
     MSKFSDIITQ LLFDAPPREI NSVYDSLVII TEDTDNDTLL DALKRCLVAK RLPIDVEGSP
     TIVTEYNKDG AKYFDPFKKV LFSVDCLDRV GLDIEPHESE TTPYQEKLYE ELQKYVAKNF
     PGDSACTVLP TGDDDELAII IVSSKFSPSN YWSGYWKSEY IYSPEERSLT GRIDVVVHYF
     EDGNVKFSTQ EFIDKEDIND PISCIRALES EIETGLDESF SKLNQTQFAK LRRKLPVTRS
     KVNWGKAISN YRLGKDAAQG K