EIF3H_XENTR
ID EIF3H_XENTR Reviewed; 335 AA.
AC Q6P381;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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; BC064151; AAH64151.1; -; mRNA.
DR RefSeq; NP_989359.1; NM_204028.1.
DR AlphaFoldDB; Q6P381; -.
DR SMR; Q6P381; -.
DR STRING; 8364.ENSXETP00000035384; -.
DR MEROPS; M67.971; -.
DR PaxDb; Q6P381; -.
DR GeneID; 394989; -.
DR KEGG; xtr:394989; -.
DR CTD; 8667; -.
DR Xenbase; XB-GENE-958115; eif3h.
DR eggNOG; KOG1560; Eukaryota.
DR InParanoid; Q6P381; -.
DR OrthoDB; 976469at2759; -.
DR PhylomeDB; Q6P381; -.
DR Reactome; R-XTR-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-XTR-72649; Translation initiation complex formation.
DR Reactome; R-XTR-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-XTR-72702; Ribosomal scanning and start codon recognition.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
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:0042788; C:polysomal ribosome; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
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..335
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000365180"
FT DOMAIN 22..156
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 254..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 38538 MW; 18D4D446D6561BE9 CRC64;
MAARTRETGN TATVAETAVK QVQIDGMVVL KIIKHYQEEG HGSEVVQGVL LGLVVDDRLE
ITNCFPFPQH TEDDVDFDEV QYQMEMMRSL RHVNIDHLHV GWYQSTFYGT FVSRALLDSQ
FSYQHAIEES VVLIYDPIKT GQGSLSLKAY RLTPKLMEVC KEKDFSAEGL KKANIAFEDM
FEEVPIIIKN SHLINVLAWE LDKKAPVTEK HELLNLSSSN HLEKSLQLLM DRVDELSQDI
VKYNTYLRNI SKQQQQKHQY TQRRQQENLQ RQSRGETSLP EEDVNKLFKP PVPPSRMDSL
LIAGQINTYI QHIKEFTSQN LGKLFMAEAM QDPTI