IF4H_RAT
ID IF4H_RAT Reviewed; 248 AA.
AC Q5XI72;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Eukaryotic translation initiation factor 4H;
DE Short=eIF-4H;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 1 protein homolog;
GN Name=Eif4h; Synonyms=Wbscr1;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PROTEIN SEQUENCE OF 83-109 AND 152-159, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Stimulates the RNA helicase activity of EIF4A in the
CC translation initiation complex. Binds weakly mRNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
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DR EMBL; BC083818; AAH83818.1; -; mRNA.
DR RefSeq; NP_001006958.1; NM_001006957.2.
DR AlphaFoldDB; Q5XI72; -.
DR SMR; Q5XI72; -.
DR IntAct; Q5XI72; 8.
DR STRING; 10116.ENSRNOP00000043254; -.
DR iPTMnet; Q5XI72; -.
DR PhosphoSitePlus; Q5XI72; -.
DR jPOST; Q5XI72; -.
DR PaxDb; Q5XI72; -.
DR PRIDE; Q5XI72; -.
DR GeneID; 288599; -.
DR KEGG; rno:288599; -.
DR UCSC; RGD:1359222; rat.
DR CTD; 7458; -.
DR RGD; 1359222; Eif4h.
DR VEuPathDB; HostDB:ENSRNOG00000001454; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_046195_1_0_1; -.
DR InParanoid; Q5XI72; -.
DR OMA; EPPYIAY; -.
DR OrthoDB; 1530583at2759; -.
DR PhylomeDB; Q5XI72; -.
DR TreeFam; TF313897; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
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:Q5XI72; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001454; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q5XI72; baseline and differential.
DR Genevisible; Q5XI72; RN.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0019953; P:sexual reproduction; ISO:RGD.
DR CDD; cd12401; RRM_eIF4H; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034229; eIF4H_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Methylation; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT CHAIN 2..248
FT /note="Eukaryotic translation initiation factor 4H"
FT /id="PRO_0000283702"
FT DOMAIN 42..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
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:Q15056"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 166
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
SQ SEQUENCE 248 AA; 27324 MW; 8E1BE53690380954 CRC64;
MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
QDKGGFGFRK GGPDDRGMGG SREPRGGWDS RDDFSSGYRD DFLGGRGGSR PGDRRAGPPM
GSRFRDGPPL RGSNMDFREP TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE
EVVQKEQE
