CAZA1_RAT
ID CAZA1_RAT Reviewed; 286 AA.
AC B2GUZ5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=F-actin-capping protein subunit alpha-1 {ECO:0000250|UniProtKB:P52907};
DE AltName: Full=CapZ alpha-1 {ECO:0000250|UniProtKB:P52907};
GN Name=Capza1 {ECO:0000250|UniProtKB:P52907};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI66464.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Embryonic lung {ECO:0000312|EMBL:AAI66464.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100A1, AND SUBUNIT.
RX PubMed=19452629; DOI=10.1016/j.jmb.2009.01.022;
RA Wright N.T., Cannon B.R., Wilder P.T., Morgan M.T., Varney K.M.,
RA Zimmer D.B., Weber D.J.;
RT "Solution structure of S100A1 bound to the CapZ peptide (TRTK12).";
RL J. Mol. Biol. 386:1265-1277(2009).
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 (By similarity). Interacts with S100A1. Interacts with SH3BP1;
CC recruits CAPZA1 to forming cell junctions. Interacts with CD2AP (By
CC similarity). Directly interacts with CRACD; this interaction decreases
CC binding to actin (By similarity). {ECO:0000250|UniProtKB:P52907,
CC ECO:0000269|PubMed:19452629}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19343716}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000255}.
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DR EMBL; BC166464; AAI66464.1; -; mRNA.
DR RefSeq; NP_001103095.2; NM_001109625.2.
DR AlphaFoldDB; B2GUZ5; -.
DR BMRB; B2GUZ5; -.
DR SMR; B2GUZ5; -.
DR BioGRID; 605958; 7.
DR IntAct; B2GUZ5; 2.
DR MINT; B2GUZ5; -.
DR STRING; 10116.ENSRNOP00000052868; -.
DR iPTMnet; B2GUZ5; -.
DR PhosphoSitePlus; B2GUZ5; -.
DR World-2DPAGE; 0004:B2GUZ5; -.
DR jPOST; B2GUZ5; -.
DR PaxDb; B2GUZ5; -.
DR PeptideAtlas; B2GUZ5; -.
DR PRIDE; B2GUZ5; -.
DR Ensembl; ENSRNOT00000108033; ENSRNOP00000085539; ENSRNOG00000013538.
DR GeneID; 691149; -.
DR KEGG; rno:691149; -.
DR UCSC; RGD:1587438; rat.
DR CTD; 829; -.
DR RGD; 1587438; Capza1.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; B2GUZ5; -.
DR OMA; LKVDVHY; -.
DR OrthoDB; 1200844at2759; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:B2GUZ5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013538; Expressed in thymus and 19 other tissues.
DR Genevisible; B2GUZ5; RN.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
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; ISO:RGD.
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 Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; 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 /evidence="ECO:0000250|UniProtKB:P52907"
FT /id="PRO_0000349121"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52907"
SQ SEQUENCE 286 AA; 32910 MW; 0CB060C67D9E84C0 CRC64;
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EDVDGGLKSW
RDSCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EVQTAKEFIK IIESAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
