CAZA2_MICMU
ID CAZA2_MICMU Reviewed; 286 AA.
AC Q2QL88;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=CAPZA2;
OS Microcebus murinus (Gray mouse lemur) (Lemur murinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Cheirogaleidae; Microcebus.
OX NCBI_TaxID=30608;
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; DP000022; ABB89821.1; -; Genomic_DNA.
DR RefSeq; XP_012616530.1; XM_012761076.1.
DR AlphaFoldDB; Q2QL88; -.
DR SMR; Q2QL88; -.
DR Ensembl; ENSMICT00000068185; ENSMICP00000042953; ENSMICG00000032607.
DR GeneID; 105869361; -.
DR KEGG; mmur:105869361; -.
DR CTD; 830; -.
DR GeneTree; ENSGT00950000183119; -.
DR OrthoDB; 1085166at2759; -.
DR Proteomes; UP000694394; Chromosome 11.
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; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
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;
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_0000226308"
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; 33023 MW; 279346F9E1286D23 CRC64;
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAIESW
RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAREFIK IVEAAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA