EIF3H_TAEGU
ID EIF3H_TAEGU Reviewed; 348 AA.
AC B5FY35;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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 Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
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; DQ213760; ACH43946.1; -; mRNA.
DR RefSeq; NP_001232560.1; NM_001245631.1.
DR AlphaFoldDB; B5FY35; -.
DR SMR; B5FY35; -.
DR STRING; 59729.ENSTGUP00000026856; -.
DR MEROPS; M67.971; -.
DR GeneID; 100190645; -.
DR KEGG; tgu:100190645; -.
DR CTD; 8667; -.
DR InParanoid; B5FY35; -.
DR OrthoDB; 976469at2759; -.
DR Proteomes; UP000007754; Unplaced.
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..348
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000365175"
FT DOMAIN 35..169
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 267..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 39529 MW; B0EB69AF6B979B80 CRC64;
MASRKEGSGA AGGGFGSAKG KGKAAAAGDS AVKQVQIDGL VVLKIIKHYQ EEGQGNEVVQ
GVLLGLVVDD RLEITNCFPF PQHTEDDADF DEVQYQMEMM RSLRHVNIDH LHVGWYQSTY
YGSFVTRALL DSQFSYQHAI EESVVLIYDP IKTAQGSLSL KAYRLTPKLM EVCKEKDFSP
EALKKANIAY ENMFEEVPIV IKNSYLINVM LWELEKKSAV ADRHELLSLA SSNHLGKSLQ
LLMDRVDEMS QDIVKYNTYL RNVSKQQQQK HQYQQRRQQE NIQRQSRGEP PLPEEDINKL
FKPPQPPPRM ESLLIAGQIN TYCQNIKEFN AQNLGKLFMA QALQDYNN