ID   EIF3H_SALSA             Reviewed;         344 AA.
AC   B5RI54;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007};
DE            Short=eIF3h {ECO:0000255|HAMAP-Rule:MF_03007};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 3 {ECO:0000255|HAMAP-Rule:MF_03007};
DE   AltName: Full=eIF-3-gamma;
DE   AltName: Full=eIF3 p40 subunit {ECO:0000255|HAMAP-Rule:MF_03007};
GN   Name=eif3h; Synonyms=eif3s3;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=White muscle;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC       eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC       eif3m. {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit H family. {ECO:0000255|HAMAP-
CC       Rule:MF_03007}.
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DR   EMBL; BT043978; ACH85295.1; -; mRNA.
DR   AlphaFoldDB; B5RI54; -.
DR   SMR; B5RI54; -.
DR   STRING; 8030.ENSSSAP00000067644; -.
DR   MEROPS; M67.971; -.
DR   Proteomes; UP000087266; Genome assembly.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   CDD; cd08065; MPN_eIF3h; 1.
DR   HAMAP; MF_03007; eIF3h; 1.
DR   InterPro; IPR027524; eIF3h.
DR   InterPro; IPR045810; eIF3h_C.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR10410:SF3; PTHR10410:SF3; 1.
DR   Pfam; PF19445; eIF3h_C; 1.
DR   Pfam; PF01398; JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..344
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   H"
FT                   /id="PRO_0000365178"
FT   DOMAIN          31..165
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  39415 MW;  ABED069E10B36358 CRC64;
     MATRKESTST PTAPMASTSP GATLDSPVKQ IQIEGLVVLK MIKHYQEEGQ GSEVVQGVLL
     GLVVEDRLEI TNCFPFPQHT EDDADFDEVQ YQMEMMRSLR HVNIDHLHVG WYQSTYYGSF
     VSRALLDSQF SYQHAIEESV VLIYDPIKTA QGSLSLKAYR LTPKLMEICK EKDFSAEGLK
     KAMIGFEHMF EEVPIVIKNS HLINVLMWEL EEKCTVADKH ELLNLSSSNH LEKSLQLLMD
     RVDDMSQDIV KYNTYSRNLS KQQQQKHQYT QRRQQENAQR QTRGETPLPE EDVSKMFKPP
     QPPPRMDTLL IAGQINNYCQ NVKEFTSQNL GKLFMAEALQ GHNS