IF2M_BOVIN
ID IF2M_BOVIN Reviewed; 727 AA.
AC P46198; A6QR53;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7711084; DOI=10.1016/0167-4781(95)00041-e;
RA Ma J., Farwell M.A., Burkhart W.A., Spremulli L.L.;
RT "Cloning and sequence analysis of the cDNA for bovine mitochondrial
RT translational initiation factor 2.";
RL Biochim. Biophys. Acta 1261:321-324(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L37835; AAB05558.1; -; mRNA.
DR EMBL; BC150118; AAI50119.1; -; mRNA.
DR PIR; S53707; S53707.
DR RefSeq; NP_776818.1; NM_174393.2.
DR PDB; 3IZY; EM; -; P=177-713.
DR PDBsum; 3IZY; -.
DR AlphaFoldDB; P46198; -.
DR SMR; P46198; -.
DR STRING; 9913.ENSBTAP00000020573; -.
DR PaxDb; P46198; -.
DR PRIDE; P46198; -.
DR Ensembl; ENSBTAT00000020573; ENSBTAP00000020573; ENSBTAG00000015481.
DR GeneID; 281923; -.
DR KEGG; bta:281923; -.
DR CTD; 4528; -.
DR VEuPathDB; HostDB:ENSBTAG00000015481; -.
DR VGNC; VGNC:31733; MTIF2.
DR eggNOG; KOG1145; Eukaryota.
DR GeneTree; ENSGT00900000141103; -.
DR HOGENOM; CLU_006301_5_2_1; -.
DR InParanoid; P46198; -.
DR OMA; LYAWPWP; -.
DR OrthoDB; 1124591at2759; -.
DR TreeFam; TF105682; -.
DR Proteomes; UP000009136; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IDA:HGNC-UCL.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IDA:HGNC-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0070124; P:mitochondrial translational initiation; IDA:BHF-UCL.
DR GO; GO:0032790; P:ribosome disassembly; IDA: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; Direct protein sequencing; GTP-binding; Initiation factor;
KW Mitochondrion; 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_0000014479"
FT DOMAIN 178..348
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:0000250|UniProtKB:Q91YJ5"
SQ SEQUENCE 727 AA; 81764 MW; FD703F91D9AB1F28 CRC64;
MNRKILKLEN LLRFHTICRQ LHSLCQRRML AQWRHMFSSA YAVHTAQLYT RPWQTDALLR
AALSQRRLLV TKKEKRSQKS PLPSTKSKKE VEVWLGMTVE ELARAMEKDI DCVYESLMNT
AIDIDSLETH SRLDEVWIKE VIKKSGMKLK WSKLKQDKVR ENKDAVKRPQ ADPALLIPRS
PVVTIMGHVD HGKTTLLDKL RKTQVAAMEA GGITQHIGAF LVSLPSGEKI TFLDTPGHAA
FSAMRARGTQ VTDIVILVVA ADDGVMKQTV ESIQHAKDAH VPIVLAINKC DKAEADPEKV
KKELLAYDVV CEDYGGDVQA VHVSALTGEN MMALAEATIA LAEMLELKAD PTGAVEGTVI
ESFTDKGRGP VTTAIIQRGT LRKGSILVAG KSWAKVRLMF DENGRAVNEA YPSMPVGIIG
WRDLPSAGDE ILEVESEPRA REVVDWRKYE QEQEKNKEDL KLIEEKRKEH QEAHRKDREK
YGTVHWKERS YIKYREKRQQ QPLKPKEKLE RDSNVLPVIV KGDVDGSVEA ILNVMDTYDA
SHECELDLVH FGVGDISEND VNLAETFHGV IYGFNVNAGN VIQQLAAKKG VKIKLHKIIY
RLIEDLQEEL SSRLPCIVEE HPIGEASILA TFSITEGKKK VPVAGCRVQK GQIEKQKKFK
LIRNGHVIWK GSLISLKHHK DDTSVVKTGM DCGLSLDEEK IEFKVGDAII CYEEKEVPAK
TSWDPGF
