ID   CAZA1_BOVIN             Reviewed;         286 AA.
AC   A4FUA8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=F-actin-capping protein subunit alpha-1;
DE   AltName: Full=CapZ alpha-1;
GN   Name=CAPZA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) 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. May play a role in the formation of epithelial cell
CC       junctions. {ECO:0000250|UniProtKB:P52907}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC       WASH complex, composed of F-actin-capping protein subunit alpha
CC       (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta
CC       (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. Interacts with
CC       S100B and S100A. Interacts with SH3BP1; recruits CAPZA1 to forming cell
CC       junctions. Interacts with CD2AP. Directly interacts with CRACD; this
CC       interaction decreases binding to actin (By similarity).
CC       {ECO:0000250|UniProtKB:P52907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; BT030727; ABS45043.1; -; mRNA.
DR   EMBL; BC114648; AAI14649.1; -; mRNA.
DR   RefSeq; NP_001076949.1; NM_001083480.2.
DR   AlphaFoldDB; A4FUA8; -.
DR   SMR; A4FUA8; -.
DR   CORUM; A4FUA8; -.
DR   STRING; 9913.ENSBTAP00000042551; -.
DR   PaxDb; A4FUA8; -.
DR   PeptideAtlas; A4FUA8; -.
DR   PRIDE; A4FUA8; -.
DR   Ensembl; ENSBTAT00000045136; ENSBTAP00000042551; ENSBTAG00000014295.
DR   GeneID; 534656; -.
DR   KEGG; bta:534656; -.
DR   CTD; 829; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014295; -.
DR   VGNC; VGNC:26756; CAPZA1.
DR   eggNOG; KOG0836; Eukaryota.
DR   GeneTree; ENSGT00950000183119; -.
DR   HOGENOM; CLU_045161_0_0_1; -.
DR   InParanoid; A4FUA8; -.
DR   OMA; LKVDVHY; -.
DR   OrthoDB; 1200844at2759; -.
DR   TreeFam; TF314822; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000014295; Expressed in abdominal lymph node and 105 other tissues.
DR   ExpressionAtlas; A4FUA8; baseline and differential.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   CHAIN           2..286
FT                   /note="F-actin-capping protein subunit alpha-1"
FT                   /id="PRO_0000355563"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
SQ   SEQUENCE   286 AA;  32932 MW;  4E4D6EDD7BA0FC4A CRC64;
     MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
     QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW
     RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
     ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EAQTAKEFIK IIEHAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKVD WNKILSYKIG KEMQNA