CAZA2_MOUSE
ID CAZA2_MOUSE Reviewed; 286 AA.
AC P47754;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=Capza2; Synonyms=Cappa2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=9331217;
RX DOI=10.1002/(sici)1097-0169(1997)38:2<120::aid-cm2>3.0.co;2-b;
RA Hart M.C., Korshunova Y.O., Cooper J.A.;
RT "Vertebrates have conserved capping protein alpha isoforms with specific
RT expression patterns.";
RL Cell Motil. Cytoskeleton 38:120-132(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-13; 20-86 AND 104-129, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL Submitted (MAR-2008) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 20-37; 67-86 AND 194-210, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
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; U16741; AAC00567.1; -; mRNA.
DR EMBL; BC082589; AAH82589.1; -; mRNA.
DR CCDS; CCDS19926.1; -.
DR RefSeq; NP_031630.1; NM_007604.2.
DR AlphaFoldDB; P47754; -.
DR SMR; P47754; -.
DR BioGRID; 198478; 35.
DR DIP; DIP-31382N; -.
DR IntAct; P47754; 19.
DR MINT; P47754; -.
DR STRING; 10090.ENSMUSP00000015877; -.
DR iPTMnet; P47754; -.
DR PhosphoSitePlus; P47754; -.
DR SwissPalm; P47754; -.
DR REPRODUCTION-2DPAGE; P47754; -.
DR CPTAC; non-CPTAC-3771; -.
DR EPD; P47754; -.
DR jPOST; P47754; -.
DR PaxDb; P47754; -.
DR PeptideAtlas; P47754; -.
DR PRIDE; P47754; -.
DR ProteomicsDB; 265676; -.
DR Antibodypedia; 2213; 208 antibodies from 26 providers.
DR DNASU; 12343; -.
DR Ensembl; ENSMUST00000015877; ENSMUSP00000015877; ENSMUSG00000015733.
DR GeneID; 12343; -.
DR KEGG; mmu:12343; -.
DR UCSC; uc009azs.1; mouse.
DR CTD; 830; -.
DR MGI; MGI:106222; Capza2.
DR VEuPathDB; HostDB:ENSMUSG00000015733; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; P47754; -.
DR OMA; HVHYYED; -.
DR OrthoDB; 1085166at2759; -.
DR PhylomeDB; P47754; -.
DR TreeFam; TF314822; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 12343; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Capza2; mouse.
DR PRO; PR:P47754; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P47754; protein.
DR Bgee; ENSMUSG00000015733; Expressed in triceps brachii and 268 other tissues.
DR ExpressionAtlas; P47754; baseline and differential.
DR Genevisible; P47754; MM.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IPI:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..286
FT /note="F-actin-capping protein subunit alpha-2"
FT /id="PRO_0000208628"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47755"
SQ SEQUENCE 286 AA; 32967 MW; E706A9BC1830E70B CRC64;
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAIESW
RTSVETALRA YVKEHYPNGV CTVYGKKVDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
VTPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
