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AR1BB_XENLA
ID   AR1BB_XENLA             Reviewed;         369 AA.
AC   Q6GNU1;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 1B-B {ECO:0000305};
GN   Name=arpc1b-b; ORFNames=XELAEV_18047442mg {ECO:0000312|EMBL:OCT61419.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J;
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). In addition to its role in the cytoplasmic
CC       cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
CC       the nucleus, thereby regulating gene transcription and repair of
CC       damaged DNA. The Arp2/3 complex promotes homologous recombination (HR)
CC       repair in response to DNA damage by promoting nuclear actin
CC       polymerization, leading to drive motility of double-strand breaks
CC       (DSBs) (By similarity). {ECO:0000250|UniProtKB:O15143,
CC       ECO:0000250|UniProtKB:Q7ZXD5}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of actr2/arp2,
CC       actr3/arp3, arpc1 (arpc1a or arpc1b), arpc2, arpc3, arpc4 and arpc5.
CC       {ECO:0000250|UniProtKB:O15143}.
CC   -!- INTERACTION:
CC       Q6GNU1; Q6P5F9: Xpo1; Xeno; NbExp=2; IntAct=EBI-11607516, EBI-2550236;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q7ZXD5}. Nucleus {ECO:0000250|UniProtKB:O15143}.
CC   -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR   EMBL; CM004483; OCT61419.1; -; Genomic_DNA.
DR   EMBL; BC073411; AAH73411.1; -; mRNA.
DR   RefSeq; NP_001085837.1; NM_001092368.1.
DR   AlphaFoldDB; Q6GNU1; -.
DR   SMR; Q6GNU1; -.
DR   IntAct; Q6GNU1; 1.
DR   STRING; 8355.Q6GNU1; -.
DR   DNASU; 444264; -.
DR   GeneID; 444264; -.
DR   KEGG; xla:444264; -.
DR   CTD; 444264; -.
DR   Xenbase; XB-GENE-6255689; arpc1b.S.
DR   OMA; TLKGSTW; -.
DR   OrthoDB; 848569at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 444264; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
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; 6.
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..369
FT                   /note="Actin-related protein 2/3 complex subunit 1B-B"
FT                   /id="PRO_0000445570"
FT   REPEAT          6..45
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          50..89
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          94..135
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          140..179
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          200..239
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          242..280
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          321..364
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   369 AA;  41394 MW;  7639B1343241FDF7 CRC64;
     MAFHSFLLEP ITCHAWNKDA TQIAFCPNSH DVHIYKKDGV KWTKIHELKE HNGQVTGIDW
     APESNRIVTC GTDRNAYVWT LRNNVWKPTL VILRINRAAR CVKWSPKENK FAVGSGSRLI
     SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SSDFKSRIFS SYIKEVEERP
     APTPWGSKMP FGELMFESSS SCGWVHSVCF SNSGDRMAWV SHDSTICIAD ATKKMRVTSL
     ITDTLPLLCV TFITENSLVA AGHDCYPVLY TYDEAQGTLS FGGKLDVPKQ SSQRGMTARE
     RFQNLDKKAS SDTNNITLDS LHKNSISQIS VLSGGKAKCS KFCTTGLDGG MCIWDVKSLE
     SALKDLKIK
 
 
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