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CAZA2_CHICK
ID   CAZA2_CHICK             Reviewed;         286 AA.
AC   P28497;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=F-actin-capping protein subunit alpha-2;
DE   AltName: Full=Beta-actinin subunit I;
DE   AltName: Full=CapZ 36/32;
GN   Name=CAPZA2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver, and Muscle;
RX   PubMed=1711931; DOI=10.1002/cm.970180306;
RA   Cooper J.A., Caldwell J.E., Gattermeir D.J., Torres M.A., Amatruda J.F.,
RA   Casella J.F.;
RT   "Variant cDNAs encoding proteins similar to the alpha subunit of chicken
RT   CapZ.";
RL   Cell Motil. Cytoskeleton 18:204-214(1991).
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. CapZ may mediate the attachment of the barbed ends of
CC       actin filaments to the Z-line.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC       WASH complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line.
CC       Note=CapZ is located at the Z line in chicken muscle.
CC   -!- TISSUE SPECIFICITY: Present in all tissues examined.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; M80589; AAA48656.1; -; mRNA.
DR   PIR; S36093; S36093.
DR   RefSeq; NP_001004380.1; NM_001004380.1.
DR   AlphaFoldDB; P28497; -.
DR   SMR; P28497; -.
DR   BioGRID; 679070; 2.
DR   IntAct; P28497; 2.
DR   MINT; P28497; -.
DR   STRING; 9031.ENSGALP00000015277; -.
DR   PaxDb; P28497; -.
DR   Ensembl; ENSGALT00000053621; ENSGALP00000056878; ENSGALG00000043437.
DR   GeneID; 417771; -.
DR   KEGG; gga:417771; -.
DR   CTD; 830; -.
DR   VEuPathDB; HostDB:geneid_417771; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   GeneTree; ENSGT00950000183119; -.
DR   HOGENOM; CLU_045161_0_0_1; -.
DR   InParanoid; P28497; -.
DR   OMA; HVHYYED; -.
DR   OrthoDB; 1085166at2759; -.
DR   PhylomeDB; P28497; -.
DR   TreeFam; TF314822; -.
DR   Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-GGA-879415; Advanced glycosylation endproduct receptor signaling.
DR   Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:P28497; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000043437; Expressed in muscle tissue and 14 other tissues.
DR   ExpressionAtlas; P28497; baseline and differential.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
DR   GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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   Actin capping; Actin-binding; Cytoplasm; Direct protein sequencing;
KW   Reference proteome.
FT   CHAIN           1..286
FT                   /note="F-actin-capping protein subunit alpha-2"
FT                   /id="PRO_0000208635"
SQ   SEQUENCE   286 AA;  32845 MW;  1D08B328650EC227 CRC64;
     MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
     QFTPVKIDGY DEQVLITEHG DLGNGKFLDP KNKISFKFDH LRKEATDPRP HEVENAIESW
     RNSVETAMKA YVKEHYPNGV CTVYGKTIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
     ISPSTTQVAG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EAQTAKEFIK IVEAAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
 
 
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