EIF3H_SCHPO
ID EIF3H_SCHPO Reviewed; 357 AA.
AC Q9UT48;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
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};
GN Name=eif3h; ORFNames=SPAC821.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15904532; DOI=10.1186/1741-7007-3-14;
RA Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A.,
RA Leatherwood J., Wolf D.A.;
RT "PCI proteins eIF3e and eIF3m define distinct translation initiation factor
RT 3 complexes.";
RL BMC Biol. 3:14-14(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(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. The eIF-3 complex appears to include tif32/eif3a,
CC SPAC25G10.08/eif3b, tif33/eif3c, SPBC4C3.07/eif3f, tif35/eif3g and
CC sum1/eif3i. This set of common subunits may also associate exclusively
CC with either moe1/eif3d and int6/eif3e, or with SPAC821.05/eif3h and
CC SPAC1751.03/eif3m. The eIF-3 complex may also include
CC SPAC3A12.13c/eif3j. {ECO:0000255|HAMAP-Rule:MF_03007,
CC ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit H family. {ECO:0000255|HAMAP-
CC Rule:MF_03007}.
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DR EMBL; CU329670; CAB57439.1; -; Genomic_DNA.
DR PIR; T41716; T41716.
DR RefSeq; NP_593158.1; NM_001018556.2.
DR AlphaFoldDB; Q9UT48; -.
DR SMR; Q9UT48; -.
DR BioGRID; 279585; 196.
DR STRING; 4896.SPAC821.05.1; -.
DR iPTMnet; Q9UT48; -.
DR MaxQB; Q9UT48; -.
DR PaxDb; Q9UT48; -.
DR PRIDE; Q9UT48; -.
DR EnsemblFungi; SPAC821.05.1; SPAC821.05.1:pep; SPAC821.05.
DR GeneID; 2543153; -.
DR KEGG; spo:SPAC821.05; -.
DR PomBase; SPAC821.05; -.
DR VEuPathDB; FungiDB:SPAC821.05; -.
DR eggNOG; KOG1560; Eukaryota.
DR HOGENOM; CLU_044094_1_0_1; -.
DR InParanoid; Q9UT48; -.
DR OMA; KFNRYQQ; -.
DR PhylomeDB; Q9UT48; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q9UT48; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0008180; C:COP9 signalosome; ISS:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:PomBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:PomBase.
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:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
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 PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Nucleus; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..357
FT /note="Eukaryotic translation initiation factor 3 subunit
FT H"
FT /id="PRO_0000316244"
FT DOMAIN 20..162
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 357 AA; 39781 MW; 40060B83FBC08BE9 CRC64;
MSDTTSLNVP ELESPPIERV ELESLLVMNI IKHCRDSFPN MGTIGQLVGI DIDGVLQVSS
SFESPSVLEN EESAVNKSVS GKARQAHTEA MLNRLQYIGA VTGHVGWYLG AYVSSFLSSP
FFVETQYAYQ KANPNSIAFL YDLSQSSNGT LYMRAYQLTP EFMAAHEEKT WTASSLNSHN
LTPSNVIREL PIVIHNSHLA TCLLHSLSEP PTPASTLTAE AALEDCESNL PLTETFSNFE
VSLGTRYRKN IELLLESTDE FHYEQGNLGF HQRQLAREQA KIQQWIAKRK AENANRAAEN
LQPLPLDDWK RIFKLPAEPR LLDSLLISSQ IMKSTQIDEQ SSAFLSKLAG VRNAYAS
