ID   CAZA2_MUNMU             Reviewed;         286 AA.
AC   Q09YJ9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=F-actin-capping protein subunit alpha-2;
DE   AltName: Full=CapZ alpha-2;
GN   Name=CAPZA2;
OS   Muntiacus muntjak (Barking deer) (Indian muntjac).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Muntiacinae; Muntiacus.
OX   NCBI_TaxID=9888;
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 (SEP-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 (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; DP000178; ABI75281.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09YJ9; -.
DR   SMR; Q09YJ9; -.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
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.
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_0000260357"
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;  32979 MW;  2BAC02A6B3317631 CRC64;
     MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
     QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRISFKFDH LRKEATDPRP YEAENAIESW
     RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
     ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA