ID   IF4H_BOVIN              Reviewed;         228 AA.
AC   Q1JPH6; A5D959;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Eukaryotic translation initiation factor 4H;
DE            Short=eIF-4H;
GN   Name=EIF4H;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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; BT025377; ABF57333.1; -; mRNA.
DR   EMBL; BT030478; ABQ12918.1; -; mRNA.
DR   RefSeq; NP_001069220.1; NM_001075752.1.
DR   AlphaFoldDB; Q1JPH6; -.
DR   SMR; Q1JPH6; -.
DR   STRING; 9913.ENSBTAP00000054254; -.
DR   PaxDb; Q1JPH6; -.
DR   PeptideAtlas; Q1JPH6; -.
DR   PRIDE; Q1JPH6; -.
DR   GeneID; 517409; -.
DR   KEGG; bta:517409; -.
DR   CTD; 7458; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_046195_1_0_1; -.
DR   InParanoid; Q1JPH6; -.
DR   OrthoDB; 1530583at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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: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   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_0000283700"
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..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..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         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         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;  25219 MW;  5074AC696268B9F5 CRC64;
     MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
     IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
     QDKGGFGFRK GGPDDRGFRD DFLGGRGGSR PGDRRTGPPM GSRFRDGPPL RGPNMDFREP
     TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE EVVHKEQE