CAZA1_MOUSE
ID CAZA1_MOUSE Reviewed; 286 AA.
AC P47753; Q91YN7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=F-actin-capping protein subunit alpha-1;
DE AltName: Full=CapZ alpha-1;
GN Name=Capza1; Synonyms=Cappa1;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
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 [3]
RP PROTEIN SEQUENCE OF 194-210.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. May play a role in the formation of epithelial cell
CC junctions. {ECO:0000250|UniProtKB:P52907}.
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 S100B and S100A. Interacts with SH3BP1; recruits CAPZA1 to forming cell
CC junctions. Interacts with CD2AP. Directly interacts with CRACD; this
CC interaction decreases binding to actin (By similarity).
CC {ECO:0000250|UniProtKB:P52907}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; BC016232; AAH16232.1; -; mRNA.
DR EMBL; U16740; AAC00566.1; -; mRNA.
DR CCDS; CCDS38580.1; -.
DR PDB; 7CCC; X-ray; 3.20 A; C=1-286.
DR PDB; 7PDZ; EM; 3.80 A; F=1-286.
DR PDBsum; 7CCC; -.
DR PDBsum; 7PDZ; -.
DR AlphaFoldDB; P47753; -.
DR BMRB; P47753; -.
DR SMR; P47753; -.
DR BioGRID; 198477; 54.
DR IntAct; P47753; 26.
DR MINT; P47753; -.
DR STRING; 10090.ENSMUSP00000102381; -.
DR iPTMnet; P47753; -.
DR PhosphoSitePlus; P47753; -.
DR SwissPalm; P47753; -.
DR REPRODUCTION-2DPAGE; P47753; -.
DR EPD; P47753; -.
DR jPOST; P47753; -.
DR MaxQB; P47753; -.
DR PaxDb; P47753; -.
DR PeptideAtlas; P47753; -.
DR PRIDE; P47753; -.
DR ProteomicsDB; 265675; -.
DR MGI; MGI:106227; Capza1.
DR eggNOG; KOG0836; Eukaryota.
DR InParanoid; P47753; -.
DR PhylomeDB; P47753; -.
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; 12340; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Capza1; mouse.
DR PRO; PR:P47753; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P47753; protein.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:MGI.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
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 3D-structure; Acetylation; Actin capping; Actin-binding; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT CHAIN 2..286
FT /note="F-actin-capping protein subunit alpha-1"
FT /id="PRO_0000208625"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT CONFLICT 222
FT /note="V -> I (in Ref. 2; AAC00566)"
FT /evidence="ECO:0000305"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7CCC"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7CCC"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:7CCC"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 169..180
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:7CCC"
FT STRAND 200..216
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 221..252
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:7CCC"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7CCC"
SQ SEQUENCE 286 AA; 32940 MW; 6FE97BCE5D9B9D3A CRC64;
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNQISFKFDH LRKEASDPQP EDVDGGLKSW
RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
ITPPSAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EVQTTKEFIK IIESAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
