CAZA2_ORNAN
ID CAZA2_ORNAN Reviewed; 286 AA.
AC Q07E00;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=CAPZA2;
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258;
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; DP000185; ABI93676.1; -; Genomic_DNA.
DR RefSeq; NP_001229662.1; NM_001242733.1.
DR AlphaFoldDB; Q07E00; -.
DR SMR; Q07E00; -.
DR STRING; 9258.ENSOANP00000001390; -.
DR Ensembl; ENSOANT00000073324; ENSOANP00000041058; ENSOANG00000038071.
DR GeneID; 100079143; -.
DR KEGG; oaa:100079143; -.
DR CTD; 830; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR InParanoid; Q07E00; -.
DR OrthoDB; 1085166at2759; -.
DR Proteomes; UP000002279; Chromosome 10.
DR Bgee; ENSOANG00000038071; Expressed in endometrium and 8 other tissues.
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_0000260360"
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; 32999 MW; 6E5ED4AB6511AFC0 CRC64;
MADVEDQLSD DEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNVD
QFTPVKVEGY DEQVLITEHG DLGNGKFWDP KNRVSFKFDH LRKEATDPRP QEPENAVESW
RHSVETAMRA YVKEHYPNGV CTVYGKTIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
TAINENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA