IF4H_PONAB
ID IF4H_PONAB Reviewed; 228 AA.
AC Q5RBR8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Eukaryotic translation initiation factor 4H;
DE Short=eIF-4H;
GN Name=EIF4H;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858567; CAH90792.1; -; mRNA.
DR RefSeq; NP_001125449.1; NM_001131977.1.
DR AlphaFoldDB; Q5RBR8; -.
DR SMR; Q5RBR8; -.
DR STRING; 9601.ENSPPYP00000019605; -.
DR GeneID; 100172357; -.
DR KEGG; pon:100172357; -.
DR CTD; 7458; -.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q5RBR8; -.
DR OrthoDB; 1530583at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT CHAIN 2..228
FT /note="Eukaryotic translation initiation factor 4H"
FT /id="PRO_0000283701"
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 122..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
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 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 146
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 155
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
SQ SEQUENCE 228 AA; 25201 MW; 8B9AA84BA8A0329F CRC64;
MADFDTYDDR AYNSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
QDKGGFGFRK GGPDDRGFRD DFLGGRGGSR PGDRRTGPAM GSRFRDGPPL RGSNMDFREP
TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE EVVQKEQE