ID   CAZA2_HORSE             Reviewed;         286 AA.
AC   Q2QLA8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=F-actin-capping protein subunit alpha-2;
DE   AltName: Full=CapZ alpha-2;
GN   Name=CAPZA2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (NOV-2005) 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 (By similarity). {ECO:0000250}.
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       RCSD1/CAPZIP (By similarity). Directly interacts with CRACD; this
CC       interaction decreases binding to actin (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P47755}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; DP000020; ABB89801.1; -; Genomic_DNA.
DR   RefSeq; NP_001107614.1; NM_001114142.1.
DR   AlphaFoldDB; Q2QLA8; -.
DR   SMR; Q2QLA8; -.
DR   STRING; 9796.ENSECAP00000019129; -.
DR   PaxDb; Q2QLA8; -.
DR   PeptideAtlas; Q2QLA8; -.
DR   PRIDE; Q2QLA8; -.
DR   Ensembl; ENSECAT00000023108; ENSECAP00000019129; ENSECAG00000021693.
DR   GeneID; 100071181; -.
DR   KEGG; ecb:100071181; -.
DR   CTD; 830; -.
DR   VGNC; VGNC:16050; CAPZA2.
DR   GeneTree; ENSGT00950000183119; -.
DR   InParanoid; Q2QLA8; -.
DR   OrthoDB; 1085166at2759; -.
DR   Proteomes; UP000002281; Chromosome 4.
DR   Bgee; ENSECAG00000021693; Expressed in gluteus medius and 23 other tissues.
DR   ExpressionAtlas; Q2QLA8; baseline.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
DR   GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
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   3: Inferred from homology;
KW   Acetylation; Actin capping; Actin-binding; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P47755"
FT   CHAIN           2..286
FT                   /note="F-actin-capping protein subunit alpha-2"
FT                   /id="PRO_0000226310"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P47755"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47755"
SQ   SEQUENCE   286 AA;  32951 MW;  ABC0D5EEFFE89395 CRC64;
     MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
     QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAVESW
     RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
     ITPSTAQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA