IF5_MOUSE
ID IF5_MOUSE Reviewed; 429 AA.
AC P59325;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=Eif5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, and Eye;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-388 AND SER-417, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-387 AND SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; BC039275; AAH39275.1; -; mRNA.
DR EMBL; BC042622; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS26180.1; -.
DR RefSeq; NP_775539.1; NM_173363.5.
DR RefSeq; NP_829887.1; NM_178041.2.
DR AlphaFoldDB; P59325; -.
DR BMRB; P59325; -.
DR SMR; P59325; -.
DR BioGRID; 229973; 34.
DR IntAct; P59325; 3.
DR MINT; P59325; -.
DR STRING; 10090.ENSMUSP00000126825; -.
DR CarbonylDB; P59325; -.
DR iPTMnet; P59325; -.
DR PhosphoSitePlus; P59325; -.
DR SwissPalm; P59325; -.
DR EPD; P59325; -.
DR jPOST; P59325; -.
DR PaxDb; P59325; -.
DR PeptideAtlas; P59325; -.
DR PRIDE; P59325; -.
DR ProteomicsDB; 269379; -.
DR Antibodypedia; 47; 268 antibodies from 33 providers.
DR DNASU; 217869; -.
DR Ensembl; ENSMUST00000050993; ENSMUSP00000061616; ENSMUSG00000021282.
DR Ensembl; ENSMUST00000166123; ENSMUSP00000126825; ENSMUSG00000021282.
DR Ensembl; ENSMUST00000222375; ENSMUSP00000152791; ENSMUSG00000021282.
DR GeneID; 217869; -.
DR KEGG; mmu:217869; -.
DR UCSC; uc007pdd.2; mouse.
DR CTD; 1983; -.
DR MGI; MGI:95309; Eif5.
DR VEuPathDB; HostDB:ENSMUSG00000021282; -.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; P59325; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; P59325; -.
DR TreeFam; TF101533; -.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 217869; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Eif5; mouse.
DR PRO; PR:P59325; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P59325; protein.
DR Bgee; ENSMUSG00000021282; Expressed in otic placode and 261 other tissues.
DR ExpressionAtlas; P59325; baseline and differential.
DR Genevisible; P59325; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:MGI.
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 GTP-binding; Initiation factor; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..429
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212517"
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:0000250|UniProtKB:P55010"
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:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55010"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
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; 48968 MW; C77DD5DFBB5C1DEF 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 EGIIDSSDKE IVAEAERLDV KAMGPLVLTE VLFDEKIREQ IKKYRRHFLR
FCHNNKKAQR YLLHGLECVV AMHQAQLISK IPHILKEMYD ADLLEEEVII SWSEKASKKY
VSKELAKEIR VKAEPFIKWL KEAEEESSGG EEEDEDENIE VVYSKTASVP KVETVKSDNK
DDDIDIDAI
