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CAPZB_CAEEL
ID   CAPZB_CAEEL             Reviewed;         270 AA.
AC   P34686;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=F-actin-capping protein subunit beta;
GN   Name=cap-2; ORFNames=M106.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=8257793; DOI=10.1091/mbc.4.9.907;
RA   Waddle J.A., Cooper J.A., Waterston R.H.;
RT   "The alpha and beta subunits of nematode actin capping protein function in
RT   yeast.";
RL   Mol. Biol. Cell 4:907-917(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC       {ECO:0000305}.
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DR   EMBL; Z18806; CAA79270.1; -; Genomic_DNA.
DR   EMBL; Z18854; CAA79306.1; -; mRNA.
DR   EMBL; Z46935; CAA87051.1; -; Genomic_DNA.
DR   PIR; B47734; B47734.
DR   RefSeq; NP_496336.1; NM_063935.6.
DR   AlphaFoldDB; P34686; -.
DR   SMR; P34686; -.
DR   BioGRID; 39983; 19.
DR   DIP; DIP-26957N; -.
DR   IntAct; P34686; 1.
DR   STRING; 6239.M106.5; -.
DR   EPD; P34686; -.
DR   PaxDb; P34686; -.
DR   EnsemblMetazoa; M106.5.1; M106.5.1; WBGene00000293.
DR   GeneID; 174673; -.
DR   KEGG; cel:CELE_M106.5; -.
DR   UCSC; M106.5.1; c. elegans.
DR   CTD; 174673; -.
DR   WormBase; M106.5; CE01608; WBGene00000293; cap-2.
DR   eggNOG; KOG3174; Eukaryota.
DR   GeneTree; ENSGT00390000017957; -.
DR   HOGENOM; CLU_045864_1_1_1; -.
DR   InParanoid; P34686; -.
DR   OMA; MIEDMEI; -.
DR   OrthoDB; 1076134at2759; -.
DR   PhylomeDB; P34686; -.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR   Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR   Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:P34686; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000293; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005869; C:dynactin complex; IDA:WormBase.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:WormBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0000578; P:embryonic axis specification; IMP:WormBase.
DR   GO; GO:0051490; P:negative regulation of filopodium assembly; IBA:GO_Central.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR   Gene3D; 1.20.58.570; -; 1.
DR   Gene3D; 3.90.1150.210; -; 1.
DR   InterPro; IPR037282; CapZ_alpha/beta.
DR   InterPro; IPR042276; CapZ_alpha/beta_2.
DR   InterPro; IPR001698; CAPZB.
DR   InterPro; IPR043175; CAPZB_N.
DR   InterPro; IPR019771; F-actin_capping_bsu_CS.
DR   PANTHER; PTHR10619; PTHR10619; 1.
DR   Pfam; PF01115; F_actin_cap_B; 1.
DR   PRINTS; PR00192; FACTINCAPB.
DR   SUPFAM; SSF90096; SSF90096; 1.
DR   PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..270
FT                   /note="F-actin-capping protein subunit beta"
FT                   /id="PRO_0000204637"
SQ   SEQUENCE   270 AA;  30786 MW;  8EB7BC108233CDC1 CRC64;
     MGEQQLDCAL DLMRRLPPQH CDKNLTDLID LCPHLVDDLL STIDQPLKIA ADRETGKQYL
     LCDYNRDGDS YRSPWSNTYD PPLEDGQLPS EKRRKMEIEA NAAFESYRDL YFEGGVSSVY
     FWDLDNGGFA GIVLIKKEGD GAKNITGCWD SIHVIEITER ARQAHYKLTS TIMLWLQTNK
     SSSGVMNLGG SLTRQHEMDA PINDQNTHLA NMGRMIEDQE SKMRLTINEI YFGKTKKVMS
     DLRSTEKQSE LEKQDEIVRE LNNAMANRGN
 
 
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