EIF3M_DROME
ID EIF3M_DROME Reviewed; 387 AA.
AC Q7JVI3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
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};
DE AltName: Full=Transport and Golgi organization protein 7 {ECO:0000255|HAMAP-Rule:MF_03012};
DE Short=Tango-7 {ECO:0000255|HAMAP-Rule:MF_03012};
GN Name=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
GN Synonyms=Tango7 {ECO:0000255|HAMAP-Rule:MF_03012}; ORFNames=CG8309;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16452979; DOI=10.1038/nature04377;
RA Bard F., Casano L., Mallabiabarrena A., Wallace E., Saito K., Kitayama H.,
RA Guizzunti G., Hu Y., Wendler F., Dasgupta R., Perrimon N., Malhotra V.;
RT "Functional genomics reveals genes involved in protein secretion and Golgi
RT organization.";
RL Nature 439:604-607(2006).
RN [5]
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 (Potential). {ECO:0000255|HAMAP-Rule:MF_03012}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. The eIF-3 complex interacts with pix.
CC {ECO:0000255|HAMAP-Rule:MF_03012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012,
CC ECO:0000269|PubMed:16452979}. Golgi apparatus {ECO:0000255|HAMAP-
CC Rule:MF_03012, ECO:0000269|PubMed:16452979}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC Rule:MF_03012}.
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DR EMBL; AE013599; AAF58289.1; -; Genomic_DNA.
DR EMBL; AY118924; AAM50784.1; -; mRNA.
DR RefSeq; NP_001286407.1; NM_001299478.1.
DR RefSeq; NP_610932.1; NM_137088.4.
DR AlphaFoldDB; Q7JVI3; -.
DR SMR; Q7JVI3; -.
DR BioGRID; 62316; 29.
DR IntAct; Q7JVI3; 8.
DR MINT; Q7JVI3; -.
DR STRING; 7227.FBpp0086705; -.
DR PaxDb; Q7JVI3; -.
DR PRIDE; Q7JVI3; -.
DR DNASU; 36565; -.
DR EnsemblMetazoa; FBtr0087579; FBpp0086705; FBgn0033902.
DR EnsemblMetazoa; FBtr0339964; FBpp0308985; FBgn0033902.
DR GeneID; 36565; -.
DR KEGG; dme:Dmel_CG8309; -.
DR CTD; 10480; -.
DR FlyBase; FBgn0033902; eIF3m.
DR VEuPathDB; VectorBase:FBgn0033902; -.
DR eggNOG; KOG2753; Eukaryota.
DR GeneTree; ENSGT00390000004456; -.
DR HOGENOM; CLU_035254_1_0_1; -.
DR InParanoid; Q7JVI3; -.
DR OMA; REDAQRC; -.
DR OrthoDB; 679771at2759; -.
DR PhylomeDB; Q7JVI3; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; Q7JVI3; -.
DR BioGRID-ORCS; 36565; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36565; -.
DR PRO; PR:Q7JVI3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033902; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q7JVI3; baseline and differential.
DR Genevisible; Q7JVI3; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
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:FlyBase.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0070865; C:investment cone; IDA:FlyBase.
DR GO; GO:0089720; F:caspase binding; IPI:FlyBase.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; ISS:FlyBase.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:FlyBase.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0006412; P:translation; ISS:FlyBase.
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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR Pfam; PF18005; eIF3m_C_helix; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Golgi apparatus; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..387
FT /note="Eukaryotic translation initiation factor 3 subunit
FT M"
FT /id="PRO_0000308202"
FT DOMAIN 181..340
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 387 AA; 44087 MW; F750DEEAA6E4A017 CRC64;
MTSHPVFIDL SLDEQVQELR KYFKKLGAEI SSEKSNKGVE DDLHKIIGVC DVCFKDGEPS
QIDGILNSIV SIMITIPLDR GENIVLAYCE KMTKAPNLPL GKVCLQSLWR LFNNLDTASP
LRYHVYYHLV QVAKQCEQVL EVFSGVDQLK SQFANCPPSS EQMQKLYRLL HDVTKDTNLE
LSSKVMIELL GTYTADNACV AREDAMKCIV TALADPNTFL LDPLLSLKPV RFLEGDLIHD
LLSIFVSEKL PAYVQFYEDH REFVNSQGLN HEQNMKKMRL LTFMQLAESS PEMTFETLTK
ELQINEDEVE PFVIEVLKTK LVRARLDQAN QKVHISSTMH RTFGAPQWEQ LRDLLQAWKE
NLSTVREGLT SVSSAQLDLA RSQKLIH
