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EIF3H_XENLA
ID   EIF3H_XENLA             Reviewed;         334 AA.
AC   Q5PPY6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; BC087438; AAH87438.1; -; mRNA.
DR   RefSeq; NP_001088779.1; NM_001095310.1.
DR   AlphaFoldDB; Q5PPY6; -.
DR   SMR; Q5PPY6; -.
DR   BioGRID; 106123; 2.
DR   IntAct; Q5PPY6; 1.
DR   MEROPS; M67.971; -.
DR   DNASU; 496043; -.
DR   GeneID; 496043; -.
DR   KEGG; xla:496043; -.
DR   CTD; 496043; -.
DR   Xenbase; XB-GENE-958120; eif3h.S.
DR   OrthoDB; 976469at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 496043; Expressed in oocyte and 19 other tissues.
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..334
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   H"
FT                   /id="PRO_0000365179"
FT   DOMAIN          21..155
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          247..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  38391 MW;  4ED0CBC588A009F7 CRC64;
     MAARKETGNT APIAETAVKQ VQIDGLVVLK IIKHYQEEGH GSEVVQGVLL GLVVDDRLEI
     TNCFPFPQHT EDDVDFDEVQ YQMEMMRSLR HVNIDHLHVG WYQSTFYGTF VSRALLDSQF
     SYQHAIEESV VLIYDPIKTS QGSLSLKAYR LTPKLMEICK EKDFSAEGLK KANVAYEDMF
     EEVPIVIKNS HLINVLVWEL DKKAPVTEKH ELLNLSSSNH LEKSLQLLMD RVDEMSQDIV
     KYNTYQRNVG KQQQQKHQYT QRKQQENLQR LSRGETPLPE EDVNKMFKPP VTPSRMDPLL
     IAGQINTYIQ HIKGFTSQNL GKLFMAEALQ DQTN
 
 
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