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EI2BD_RABIT
ID   EI2BD_RABIT             Reviewed;         523 AA.
AC   P41111;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Translation initiation factor eIF-2B subunit delta;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit delta;
GN   Name=EIF2B4; Synonyms=EIF2BD;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=8110836; DOI=10.1016/0167-4781(94)90037-x;
RA   Price N.T., Francia G., Hall L., Proud C.G.;
RT   "Guanine nucleotide exchange factor for eukaryotic initiation factor-2.
RT   Cloning of cDNA for the delta-subunit of rabbit translation initiation
RT   factor-2B.";
RL   Biochim. Biophys. Acta 1217:207-210(1994).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC       bound GDP for GTP.
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC       and epsilon.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA53204.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X75451; CAA53204.1; ALT_INIT; mRNA.
DR   PIR; S42727; S42727.
DR   RefSeq; NP_001076241.1; NM_001082772.1.
DR   AlphaFoldDB; P41111; -.
DR   SMR; P41111; -.
DR   STRING; 9986.ENSOCUP00000022102; -.
DR   PRIDE; P41111; -.
DR   GeneID; 100009560; -.
DR   KEGG; ocu:100009560; -.
DR   CTD; 8890; -.
DR   eggNOG; KOG1467; Eukaryota.
DR   InParanoid; P41111; -.
DR   OrthoDB; 797227at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   CHAIN           2..523
FT                   /note="Translation initiation factor eIF-2B subunit delta"
FT                   /id="PRO_0000156069"
FT   REGION          1..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
SQ   SEQUENCE   523 AA;  57121 MW;  057895B1E9D25558 CRC64;
     MAAVAVAVRE DSGSGMKAEL SARPGAGGKE MTQEEKLQLR KEKKQQKKKR KEEKGTDVDT
     ASAVSAAQCP GPAREAPGPG SQSSTPGEKV PAGRTKAELR AERRAKQEAE RALKQARKGE
     QGGPPPQASP STAGEAPAGG KRLTEHTQAD DPTLLRRLVR KSERQQVPTR KDYGSKVSLF
     SHLPQYSRQN SLTQYMSIPS SVIHPAMVRL GLQYSQGLIS GSNARCIALL RALQQVIQDY
     TTPPNEELSR DLVNKLKPYI CFLTQCRPLS ASMYNAIKFL NKEITGVSST KREEEAKAEL
     QAAADRYVQE KIVLAAQAIL RFASKKISNG DVILVYGCSS LVSRILQEAW SEGRKFRVVV
     VDSRPRLEGR HMLRFLVRAG VPASYLLIPA ASYVLPEVSK VLLGAHALLA NGSVMSRVGT
     AQLALVARAH NVPVLVCCET YKFCERVQTD AFVSNELDDP DDLQCERGDH VALANWQSHP
     SLRLLNLVYD VTPPELVDLV ITELGMIPCS SVPVVLRVKS SDQ
 
 
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