ID   CAPZA_CAEEL             Reviewed;         282 AA.
AC   P34685;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=F-actin-capping protein subunit alpha;
GN   Name=cap-1; ORFNames=D2024.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=8257793; DOI=10.1091/mbc.4.9.907;
RA   Waddle J.A., Cooper J.A., Waterston R.H.;
RT   "The alpha and beta subunits of nematode actin capping protein function in
RT   yeast.";
RL   Mol. Biol. Cell 4:907-917(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; Z18805; CAA79269.1; -; Genomic_DNA.
DR   EMBL; Z18853; CAA79305.1; -; mRNA.
DR   EMBL; FO080386; CCD63359.1; -; Genomic_DNA.
DR   PIR; A47734; A47734.
DR   RefSeq; NP_501145.1; NM_068744.3.
DR   AlphaFoldDB; P34685; -.
DR   SMR; P34685; -.
DR   BioGRID; 42616; 14.
DR   IntAct; P34685; 1.
DR   STRING; 6239.D2024.6; -.
DR   EPD; P34685; -.
DR   PaxDb; P34685; -.
DR   PeptideAtlas; P34685; -.
DR   PRIDE; P34685; -.
DR   EnsemblMetazoa; D2024.6.1; D2024.6.1; WBGene00000292.
DR   GeneID; 177497; -.
DR   KEGG; cel:CELE_D2024.6; -.
DR   UCSC; D2024.6.2; c. elegans.
DR   CTD; 177497; -.
DR   WormBase; D2024.6; CE04295; WBGene00000292; cap-1.
DR   eggNOG; KOG0836; Eukaryota.
DR   GeneTree; ENSGT00950000183119; -.
DR   HOGENOM; CLU_045161_0_0_1; -.
DR   InParanoid; P34685; -.
DR   OMA; HVHYYED; -.
DR   OrthoDB; 1085166at2759; -.
DR   PhylomeDB; P34685; -.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:P34685; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000292; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005869; C:dynactin complex; IDA:WormBase.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Reference proteome.
FT   CHAIN           1..282
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000208637"
SQ   SEQUENCE   282 AA;  32181 MW;  A0E98D5616138B89 CRC64;
     MSEISDAEKV RIASDFIKHA PPGEFNEVFN SVRMLLENDD LLKNKCVNAI AQYNVGQFVP
     VKLDGVAKQT LITPYNDLGN GRFYDEVSKK SFKYDHVRKE AADLQPHPAE SGITEQWRQA
     LQTQLDIYID DHYAKSGTGV VFARNGVFTI CIESHQFQPK NFCNGRWRSE WNVPVGDGKS
     GSQEMKGKIL SQVHYYEDGN VQLFSEKEPV LKVNVSADFD KTAKEIIHAI SEEETIYQNA
     VQENYANMSD TTFKALRRQL PVTRAKMDWN KAQTYRIGQE MK