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ARC1B_RAT
ID   ARC1B_RAT               Reviewed;         372 AA.
AC   O88656;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 1B;
DE   AltName: Full=Arp2/3 complex 41 kDa subunit;
DE   AltName: Full=p41-ARC;
GN   Name=Arpc1b;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Sehl P.D., Tai T.N., Brown L.B., Renhui Y., Kuo A., Hongkui J., Hamner M.,
RA   Goddard A., Lowe D.G.;
RT   "Identity and expression of genes in a time course of post myocardial
RT   infarction.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   IDENTIFICATION BY MASS 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).
CC   -!- FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that
CC       mediates actin polymerization upon stimulation by nucleation-promoting
CC       factor (NPF). The Arp2/3 complex mediates the formation of branched
CC       actin networks in the cytoplasm, providing the force for cell motility.
CC       In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3
CC       complex also promotes actin polymerization in the nucleus, thereby
CC       regulating gene transcription and repair of damaged DNA. The Arp2/3
CC       complex promotes homologous recombination (HR) repair in response to
CC       DNA damage by promoting nuclear actin polymerization, leading to drive
CC       motility of double-strand breaks (DSBs).
CC       {ECO:0000250|UniProtKB:O15143}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
CC       ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
CC       and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:O15143}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:O15143}. Nucleus {ECO:0000250|UniProtKB:O15143}.
CC   -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR   EMBL; AF083269; AAC32605.1; -; mRNA.
DR   EMBL; BC062027; AAH62027.1; -; mRNA.
DR   RefSeq; NP_062162.1; NM_019289.2.
DR   AlphaFoldDB; O88656; -.
DR   SMR; O88656; -.
DR   IntAct; O88656; 1.
DR   STRING; 10116.ENSRNOP00000001315; -.
DR   iPTMnet; O88656; -.
DR   PhosphoSitePlus; O88656; -.
DR   jPOST; O88656; -.
DR   PaxDb; O88656; -.
DR   PeptideAtlas; O88656; -.
DR   PRIDE; O88656; -.
DR   Ensembl; ENSRNOT00000114214; ENSRNOP00000091680; ENSRNOG00000000991.
DR   GeneID; 54227; -.
DR   KEGG; rno:54227; -.
DR   CTD; 10095; -.
DR   RGD; 2155; Arpc1b.
DR   eggNOG; KOG1523; Eukaryota.
DR   GeneTree; ENSGT00950000183183; -.
DR   HOGENOM; CLU_034396_1_0_1; -.
DR   InParanoid; O88656; -.
DR   OMA; TLKGSTW; -.
DR   OrthoDB; 848569at2759; -.
DR   PhylomeDB; O88656; -.
DR   Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   PRO; PR:O88656; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000000991; Expressed in spleen and 19 other tissues.
DR   Genevisible; O88656; RN.
DR   GO; GO:0005885; C:Arp2/3 protein complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0036284; C:tubulobulbar complex; IDA:RGD.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR030141; ARC1B.
DR   InterPro; IPR017383; ARPC1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10709; PTHR10709; 1.
DR   PANTHER; PTHR10709:SF10; PTHR10709:SF10; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..372
FT                   /note="Actin-related protein 2/3 complex subunit 1B"
FT                   /id="PRO_0000050857"
FT   REPEAT          6..45
FT                   /note="WD 1"
FT   REPEAT          50..89
FT                   /note="WD 2"
FT   REPEAT          94..135
FT                   /note="WD 3"
FT   REPEAT          140..179
FT                   /note="WD 4"
FT   REPEAT          242..280
FT                   /note="WD 5"
FT   REPEAT          324..367
FT                   /note="WD 6"
SQ   SEQUENCE   372 AA;  41057 MW;  A538CF67C8610E25 CRC64;
     MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWNKVHELKE HNGQVTGIDW
     APESNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR CVRWAPNENK FAVGSGSRVI
     SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRIFS AYIKEVEERP
     APTPWGSKMP FGELMFESSS SCGWVHGVCF SAGGSRVAWV SHDSTVCLVD AEKKMAVATL
     ASETLPLLAI TFITENSLVA AGHDCFPVLF TYDNAAGTLS FGGRLDVPKQ NSQRGLTARE
     RFQNLDKKAS SEGGAATGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM DGGMSIWDVK
     SLESALKDLK IR
 
 
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