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EIF3B_XENLA
ID   EIF3B_XENLA             Reviewed;         688 AA.
AC   Q569Z1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
GN   Name=eif3b;
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 MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC       eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC       eif3m. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; BC092246; AAH92246.1; -; mRNA.
DR   RefSeq; NP_001090004.1; NM_001096535.1.
DR   AlphaFoldDB; Q569Z1; -.
DR   SMR; Q569Z1; -.
DR   BioGRID; 592856; 2.
DR   IntAct; Q569Z1; 1.
DR   DNASU; 735075; -.
DR   GeneID; 735075; -.
DR   KEGG; xla:735075; -.
DR   CTD; 735075; -.
DR   Xenbase; XB-GENE-963855; eif3b.L.
DR   OrthoDB; 1194797at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 735075; Expressed in lung and 19 other tissues.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..688
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363787"
FT   DOMAIN          61..144
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          164..206
FT                   /note="WD 1"
FT   REPEAT          208..246
FT                   /note="WD 2"
FT   REPEAT          248..293
FT                   /note="WD 3"
FT   REPEAT          297..335
FT                   /note="WD 4"
FT   REPEAT          338..373
FT                   /note="WD 5"
FT   REPEAT          436..492
FT                   /note="WD 6"
FT   REPEAT          525..570
FT                   /note="WD 7"
FT   REPEAT          635..680
FT                   /note="WD 8"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          589..640
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   COMPBIAS        9..43
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  80256 MW;  9BA7F810CBC4134D CRC64;
     MLESERPERD MEEEGEESNE EEEEEGMSFS DPEGFEDDIS DEELLGDILK DRPQEADGID
     SVIVVDNVPQ VGPDRLEKLK NVIVKIFSKF GKLTNEFYPQ AEGSTKGYIF LEYALPAQAQ
     DAVKNADGYK LDKQHTFRVN LFTDFDKYMV IGDEWDVPEK QPFKDFGNLR SWLEDPDCRD
     QFSVIYESGD RTSIFWTDVK EPVPVEERAR WTETYVRWSP KGTYLATFHQ RGIALWGGEK
     FKQIQRFSHQ GVQLIDFSPC ERYLVTFSPL MDTKEEPQAI IIWDILTGHN KRGFHCESSA
     HWPIFKWSHD GKFFARMTLD TLSIYETPSM GLLDKKSLKI TGIKDFSWSP GGNIIAFWVP
     EDKDIPARVT LMQMPTRQEI RVRNLFNVVD CKLHWQKNGD YLCVKVDRTP KGTQGMVTNF
     EIFRMREKQV PVDVVEMKDG IIAFAWEPNG SKFAVLHGEV PRISVSFYHV KNNGKIELIK
     MYDKQQANTI FWSPQGQFLV LAGLRSMNGA LAFVDTSDCT IMNIAEHYTA SDVEWDPTGR
     YVITSVSWWS HKVDNAYWMW TFQGRLLQKN NKDRFCQLLW RPRPPSLLSQ DQIKQIKKDL
     KKYSKIFEQK DRLSQTKASK ELIERRRAMM EEYKTYREMA TKLYMEQKTA RLEIRGGVDT
     DLLDSNVEDW EEETIEFFVT EEIIPVEE
 
 
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