EIF3M_SCHPO
ID EIF3M_SCHPO Reviewed; 402 AA.
AC Q09722; Q9URK6; Q9US29;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
DE Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
GN Name=eif3m; Synonyms=csn72, csn7b; ORFNames=SPAC1751.03, SPAC31A2.01;
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 [MRNA].
RA Kawamukai M.;
RT "S. pombe hypothetical protein.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [4]
RP IDENTIFICATION.
RX PubMed=17403899; DOI=10.1128/mcb.01724-06;
RA Luke-Glaser S., Roy M., Larsen B., Le Bihan T., Metalnikov P., Tyers M.,
RA Peter M., Pintard L.;
RT "CIF-1, a shared subunit of the COP9/signalosome and eukaryotic initiation
RT factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans
RT embryo.";
RL Mol. Cell. Biol. 27:4526-4540(2007).
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_03012, ECO:0000269|PubMed:15904532}.
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_03012,
CC ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012,
CC ECO:0000269|PubMed:15904532}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC Rule:MF_03012}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31742.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB016218; BAA31742.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAB61449.1; -; Genomic_DNA.
DR PIR; T43387; T43387.
DR PIR; T50090; T50090.
DR RefSeq; NP_592913.2; NM_001018314.2.
DR AlphaFoldDB; Q09722; -.
DR SMR; Q09722; -.
DR BioGRID; 278812; 13.
DR STRING; 4896.SPAC1751.03.1; -.
DR iPTMnet; Q09722; -.
DR MaxQB; Q09722; -.
DR PaxDb; Q09722; -.
DR PRIDE; Q09722; -.
DR EnsemblFungi; SPAC1751.03.1; SPAC1751.03.1:pep; SPAC1751.03.
DR GeneID; 2542347; -.
DR KEGG; spo:SPAC1751.03; -.
DR PomBase; SPAC1751.03; -.
DR VEuPathDB; FungiDB:SPAC1751.03; -.
DR eggNOG; KOG2753; Eukaryota.
DR HOGENOM; CLU_035254_0_1_1; -.
DR InParanoid; Q09722; -.
DR OMA; VFGKHEW; -.
DR PhylomeDB; Q09722; -.
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:Q09722; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IMP:PomBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR HAMAP; MF_03012; eIF3m; 1.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR027528; eIF3m.
DR InterPro; IPR040750; eIF3m_C_helix.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR Pfam; PF18005; eIF3m_C_helix; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..402
FT /note="Eukaryotic translation initiation factor 3 subunit
FT M"
FT /id="PRO_0000121006"
FT DOMAIN 188..347
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 402 AA; 45085 MW; CD972E781BFC0A3C CRC64;
MEGSDFILVV DSSVEEQVEE LAMYLDNLEA NTDKNVLALC REYLASENVK EVLNLFLTRL
PLLAQAPEKE LEPILAVFIN LIQESAAFED HVSKFCQALE QIADQNNNLT PAILSVLSIL
FNTAVKERQH ARLSILTSVV TLTTRYSLFS TLAPNLKYFP DWLKEAGVSV SDHRAFNIFV
SKAIQSYDDE QSFAFLLEAV KMDNSTADEA VRELVQRAVN SPKYFFFDDI VTLPPVQQLE
QSTLQLLGIL SGGMTDDYVS WVAENHAHCQ HQKFDEDAIA RKMKLLTIAS LATQAPNNTL
SYGDVAKSLK IDENEVELWI IDVIRAGLVE GRMSQLTKTL SIHRSSYRVF GKHEWVALHE
KLAKWGSSLR YMLQVMEQPL SSFTIASSKK GNRDGSAVTA SE
