EIF3H_BOVIN
ID EIF3H_BOVIN Reviewed; 352 AA.
AC Q56JZ5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 {ECO:0000255|HAMAP-Rule:MF_03007};
GN Synonyms=EIF3S3 {ECO:0000255|HAMAP-Rule:MF_03007};
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].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis. The eIF-3 complex associates with the 40S
CC ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation. The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression.
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. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the
CC interaction leads to protein translation inhibitions in a
CC ubiquitination-dependent manner. Interacts with DHX33; the interaction
CC is independent of RNA (By similarity). {ECO:0000250|UniProtKB:O15372,
CC 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; AY911332; AAW82100.1; -; mRNA.
DR EMBL; BC102096; AAI02097.1; -; mRNA.
DR RefSeq; NP_001020493.1; NM_001025322.2.
DR AlphaFoldDB; Q56JZ5; -.
DR SMR; Q56JZ5; -.
DR STRING; 9913.ENSBTAP00000018645; -.
DR MEROPS; M67.971; -.
DR PaxDb; Q56JZ5; -.
DR PRIDE; Q56JZ5; -.
DR Ensembl; ENSBTAT00000018645; ENSBTAP00000018645; ENSBTAG00000014032.
DR GeneID; 506873; -.
DR KEGG; bta:506873; -.
DR CTD; 8667; -.
DR VEuPathDB; HostDB:ENSBTAG00000014032; -.
DR VGNC; VGNC:28398; EIF3H.
DR eggNOG; KOG1560; Eukaryota.
DR GeneTree; ENSGT00730000111042; -.
DR HOGENOM; CLU_044094_0_0_1; -.
DR InParanoid; Q56JZ5; -.
DR OMA; KFNRYQQ; -.
DR OrthoDB; 976469at2759; -.
DR TreeFam; TF101504; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000014032; Expressed in vas deferens and 104 other tissues.
DR ExpressionAtlas; Q56JZ5; baseline and differential.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
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:Ensembl.
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:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
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; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..352
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000231002"
FT DOMAIN 39..173
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15372"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15372, ECO:0000255|HAMAP-
FT Rule:MF_03007"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15372"
SQ SEQUENCE 352 AA; 39906 MW; 29D678DEC880CE8E CRC64;
MASRKEGTGS SATSSSSTTG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT
EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ MEMMRSLRHV NIDHLHVGWY
QSTYYGSFVT RALLDSQFSY QHAIEESVVL IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK
DFSPEALKKG NITFEHMFEE VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG
KTLQLLMDRV DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED
LSKLFKPHQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY NS
