ID   CAZA1_XENLA             Reviewed;         256 AA.
AC   P25229;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=F-actin-capping protein subunit alpha-1;
DE   AltName: Full=Actin-binding protein chain A;
DE            Short=ABP-A;
DE   Flags: Fragment;
GN   Name=capza1; Synonyms=capza;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Oocyte;
RX   PubMed=2689884; DOI=10.1038/342822a0;
RA   Ankenbauer T., Kleinschmidt J.A., Walsh M.J., Weiner O.H., Franke W.W.;
RT   "Identification of a widespread nuclear actin binding protein.";
RL   Nature 342:822-825(1989).
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 (PubMed:2689884). May play a role in the formation of
CC       epithelial cell junctions (By similarity).
CC       {ECO:0000250|UniProtKB:P52907, ECO:0000269|PubMed:2689884}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC       WASH complex (By similarity). {ECO:0000250|UniProtKB:P52907}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X51605; CAA35948.1; -; mRNA.
DR   PIR; S07105; S07105.
DR   AlphaFoldDB; P25229; -.
DR   SMR; P25229; -.
DR   IntAct; P25229; 1.
DR   MINT; P25229; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR   GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Actin-binding; Direct protein sequencing; Nucleus; Reference proteome.
FT   CHAIN           <1..256
FT                   /note="F-actin-capping protein subunit alpha-1"
FT                   /id="PRO_0000208636"
FT   NON_TER         1
SQ   SEQUENCE   256 AA;  29427 MW;  CF466225B9B97FF4 CRC64;
     EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPAKIEGY DDQVLITEHG DLGNSRFLDP
     RNRITFKFDH LRKEASDPHP DDSDVALKSW RDACDLALRA YVKEHYPNGV CTVYGKTIDG
     QQTIVSCIES HQFQPKNFWN GRWRSEWKFT ISGSTAQLVG VLKIQVHYYE DGNVQLVSHK
     DVQESITISG EAQTAKEFVK IIEQAESDYQ TAISENYQTM SDTTFKALRR QLPVTRTKID
     WNKILSYKIG KEMQNA