ID   A0A158PFZ7_ANGCS        Unreviewed;       256 AA.
AC   A0A158PFZ7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|ARBA:ARBA00014038, ECO:0000256|RuleBase:RU365077};
GN   ORFNames=ACOC_LOCUS4632 {ECO:0000313|EMBL:VDM56217.1};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000463101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0000463101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM56217.1, ECO:0000313|Proteomes:UP000267027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Costa Rica {ECO:0000313|EMBL:VDM56217.1,
RC   ECO:0000313|Proteomes:UP000267027};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU365077}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|ARBA:ARBA00011355, ECO:0000256|RuleBase:RU365077}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000256|ARBA:ARBA00010479, ECO:0000256|RuleBase:RU365077}.
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DR   EMBL; UYYA01003822; VDM56217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158PFZ7; -.
DR   STRING; 334426.A0A158PFZ7; -.
DR   WBParaSite; ACOC_0000463101-mRNA-1; ACOC_0000463101-mRNA-1; ACOC_0000463101.
DR   OMA; VACIEDH; -.
DR   Proteomes; UP000050601; Unplaced.
DR   Proteomes; UP000267027; Unassembled WGS sequence.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1140.60; F-actin capping protein, alpha subunit; 1.
DR   Gene3D; 3.90.1150.210; F-actin capping protein, beta subunit; 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; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10653:SF0; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 1.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|RuleBase:RU365077};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU365077};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267027}.
SQ   SEQUENCE   256 AA;  29160 MW;  DC3FB24A02B1ABC0 CRC64;
     MTSEVTIPDS EKIRIVSDFL QHAPPGEFNE VFNAVRMLLN NDQLLKEGCS QAVVRYNESQ
     FAPVKLDGVE KQTLITAFND IGGGRYVDDA SKKSFKYDHL RKEASDIQPY PAESTALESW
     RAALQKELDI YIEEHYAKSG IGCVFVRNGN FTNGRWRSEW KIPVGDGKMG AQELIGNVKV
     QVHYYEDGNV QLFSEKDFSV KIQVTSDVDK TAKEILQSIR DEEGKYQHAV QENYASMSDN
     TFKALRRQLP NFHKPR
//