IF2M_MOUSE
ID IF2M_MOUSE Reviewed; 727 AA.
AC Q91YJ5; Q5M6W6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial;
DE Short=IF-2(Mt);
DE Short=IF-2Mt;
DE Short=IF2(mt);
DE Flags: Precursor;
GN Name=Mtif2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION AT THR-688.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 621-727.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of C-terminal domain of mitochondrial translational
RT initiation factor 2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK136344; BAE22940.1; -; mRNA.
DR EMBL; AK146961; BAE27568.1; -; mRNA.
DR EMBL; BX284634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016590; AAH16590.1; -; mRNA.
DR CCDS; CCDS24496.1; -.
DR RefSeq; NP_001269047.1; NM_001282118.1.
DR RefSeq; NP_001269048.1; NM_001282119.1.
DR RefSeq; NP_001269049.1; NM_001282120.1.
DR RefSeq; NP_598528.2; NM_133767.3.
DR RefSeq; XP_006514954.1; XM_006514891.2.
DR RefSeq; XP_006514955.1; XM_006514892.3.
DR PDB; 2CRV; NMR; -; A=621-727.
DR PDBsum; 2CRV; -.
DR AlphaFoldDB; Q91YJ5; -.
DR SMR; Q91YJ5; -.
DR BioGRID; 218311; 3.
DR IntAct; Q91YJ5; 1.
DR MINT; Q91YJ5; -.
DR STRING; 10090.ENSMUSP00000090926; -.
DR iPTMnet; Q91YJ5; -.
DR PhosphoSitePlus; Q91YJ5; -.
DR EPD; Q91YJ5; -.
DR MaxQB; Q91YJ5; -.
DR PaxDb; Q91YJ5; -.
DR PeptideAtlas; Q91YJ5; -.
DR PRIDE; Q91YJ5; -.
DR ProteomicsDB; 267094; -.
DR Antibodypedia; 1037; 82 antibodies from 19 providers.
DR DNASU; 76784; -.
DR Ensembl; ENSMUST00000020749; ENSMUSP00000020749; ENSMUSG00000020459.
DR Ensembl; ENSMUST00000093239; ENSMUSP00000090926; ENSMUSG00000020459.
DR GeneID; 76784; -.
DR KEGG; mmu:76784; -.
DR UCSC; uc007ihc.2; mouse.
DR CTD; 4528; -.
DR MGI; MGI:1924034; Mtif2.
DR VEuPathDB; HostDB:ENSMUSG00000020459; -.
DR eggNOG; KOG1145; Eukaryota.
DR GeneTree; ENSGT00900000141103; -.
DR HOGENOM; CLU_006301_5_2_1; -.
DR InParanoid; Q91YJ5; -.
DR OMA; LYAWPWP; -.
DR OrthoDB; 1124591at2759; -.
DR PhylomeDB; Q91YJ5; -.
DR TreeFam; TF105682; -.
DR BioGRID-ORCS; 76784; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Mtif2; mouse.
DR EvolutionaryTrace; Q91YJ5; -.
DR PRO; PR:Q91YJ5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91YJ5; protein.
DR Bgee; ENSMUSG00000020459; Expressed in embryonic post-anal tail and 267 other tissues.
DR ExpressionAtlas; Q91YJ5; baseline and differential.
DR Genevisible; Q91YJ5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:HGNC-UCL.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:HGNC-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0070124; P:mitochondrial translational initiation; ISS:BHF-UCL.
DR GO; GO:0032790; P:ribosome disassembly; ISS:BHF-UCL.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Initiation factor; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..727
FT /note="Translation initiation factor IF-2, mitochondrial"
FT /id="PRO_0000014481"
FT DOMAIN 178..346
FT /note="tr-type G"
FT REGION 187..194
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 212..216
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 234..237
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 288..291
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 324..326
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 187..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 234..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 288..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15378723"
FT CONFLICT 645
FT /note="G -> D (in Ref. 1; AAH16590)"
FT /evidence="ECO:0000305"
FT STRAND 622..636
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 639..651
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 674..681
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 691..695
FT /evidence="ECO:0007829|PDB:2CRV"
FT STRAND 707..712
FT /evidence="ECO:0007829|PDB:2CRV"
SQ SEQUENCE 727 AA; 81289 MW; 6BC3FDE9BB363090 CRC64;
MNQKLLKLEN LLRFHTICRQ VHSPSQRRLL AWCRHGFAPA SSVWRDLLGA RSWQTDMLIG
SALHQHRLLV TKKEKRPPRS QLSPVKTKKE VEVWVGMTVE DLASAMAKDI DCVYEALLNT
AIDVDSLEAN SHLDEVWIKE VIKKAGMKLK WSKLKQERIR ENKDAVRRPG TDPALLKPRS
PVVTVMGHVD HGKTTLLDKL RETQVAAMEV GGITQHIGAF LVSLPSGEKI TFLDTPGHAA
FSAMRARGAQ VTDIVVLVVA ADDGVMKQTV ESIQHAKDAE VPIILAINKC DKTDADPEKV
KKELLAYDVV CEEYGGDVQA VHVSALTGDN LMALAEATIA LAEILELKAD PTGPVEGTVI
ESFTDKGRGP VTTAIIQRGT LRKGSILVAG KSWAKVRLIF DENGKILNEA YPSMPVGIIG
WRDLPSAGDE ILEVESEPRA REVIEWRKSE QKEEKGKDDL KIMEEKRREH QEAHRKAREK
YGSLHWKERS YIKFLERKQQ RPLKPKEKVE RQSNVLPIII KGDVDGSVEA ILNLLDTYDA
SHECELELVH FGLGDISEND VTFAETFDGV IYGFNVEAGS AIQQSAAQKG VKIKLHKIIY
HLIEDLQEEL SSRLPHTLEE YPIGEASILA TFTVTEGKKK IPVAGCRVQK GQLERHKKFK
LIRNGQVIWK GSLTSLKHHK DDISVIKTGM DCGLSLDEEK VEFKPGDQVI CYEENKVPTK
TSWDPGF
