IF5_RAT
ID IF5_RAT Reviewed; 429 AA.
AC Q07205;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=Eif5;
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], AND PROTEIN SEQUENCE OF 131-150; 215-242 AND
RP 339-353.
RC TISSUE=Liver;
RX PubMed=8464924; DOI=10.1073/pnas.90.7.3058;
RA Das K., Chevesich J., Maitra U.;
RT "Molecular cloning and expression of cDNA for mammalian translation
RT initiation factor 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3058-3062(1993).
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 PHOSPHORYLATION AT SER-387 AND SER-388.
RX PubMed=11861906; DOI=10.1093/nar/30.5.1154;
RA Majumdar R., Bandyopadhyay A., Deng H., Maitra U.;
RT "Phosphorylation of mammalian translation initiation factor 5 (eIF5) in
RT vitro and in vivo.";
RL Nucleic Acids Res. 30:1154-1162(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-227; SER-387 AND
RP SER-388, AND 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: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]).
CC -!- SUBUNIT: Interacts with FMR1; this interaction occurs in a RNA-
CC dependent manner (By similarity). Interacts with EIF2S2 (By
CC similarity). {ECO:0000250|UniProtKB:P55010}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; L11651; AAA41112.1; -; mRNA.
DR EMBL; BC062398; AAH62398.1; -; mRNA.
DR PIR; A47305; A47305.
DR RefSeq; NP_001316808.1; NM_001329879.1.
DR RefSeq; NP_064460.1; NM_020075.1.
DR RefSeq; XP_006240671.1; XM_006240609.3.
DR RefSeq; XP_017458786.1; XM_017603297.1.
DR AlphaFoldDB; Q07205; -.
DR BMRB; Q07205; -.
DR SMR; Q07205; -.
DR BioGRID; 248584; 1.
DR IntAct; Q07205; 2.
DR STRING; 10116.ENSRNOP00000013695; -.
DR iPTMnet; Q07205; -.
DR PhosphoSitePlus; Q07205; -.
DR SwissPalm; Q07205; -.
DR jPOST; Q07205; -.
DR PaxDb; Q07205; -.
DR PRIDE; Q07205; -.
DR Ensembl; ENSRNOT00000013695; ENSRNOP00000013695; ENSRNOG00000010218.
DR GeneID; 108348073; -.
DR GeneID; 56783; -.
DR KEGG; rno:108348073; -.
DR UCSC; RGD:619861; rat.
DR CTD; 1983; -.
DR RGD; 619861; Eif5.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; Q07205; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; Q07205; -.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q07205; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000010218; Expressed in ileum and 20 other tissues.
DR Genevisible; Q07205; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IDA:RGD.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:RGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:RGD.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:RGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; GTP-binding; Initiation factor; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..429
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212518"
FT DOMAIN 231..390
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 143..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55010"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11861906,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11861906,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55010"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55010"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55010"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55010"
SQ SEQUENCE 429 AA; 48954 MW; B1A62E30936908EE CRC64;
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE
LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN
SCKACGYRGM LDTHHKLCTF ILKNPPENSD IGTGKKEKEK KNRKGKDKEN GSVSTSETPP
PPPPNEISPP HAVEEEEDDD WGEDTTEEAQ RRRMDEISDH AKGLTLSDDL ERTVEERVNI
LFDFVKKKKE EGIIDSSDKD IVAEAERLDV KAMGPLVLTE VLFDEKIREQ IKKYRRHFLR
FCHNNKKAQR YLLHGLECVV AMHQAQLISK IPHILKEMYD ADLLEEEVII SWSEKASKKY
VSKELAKEIR VKAEPFIKWL KEAEEESSGG EEEDEDENIE VVYSKTASVP KVETVKSDNK
DDDIDIDAI
