Full text data of MTIF3
MTIF3
[Confidence: low (only semi-automatic identification from reviews)]
Translation initiation factor IF-3, mitochondrial; IF-3(Mt); IF-3Mt; IF3(mt); IF3mt; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Translation initiation factor IF-3, mitochondrial; IF-3(Mt); IF-3Mt; IF3(mt); IF3mt; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H2K0
ID IF3M_HUMAN Reviewed; 278 AA.
AC Q9H2K0; Q05BL8; Q5W0V0; Q86X68;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 84.
DE RecName: Full=Translation initiation factor IF-3, mitochondrial;
DE Short=IF-3(Mt);
DE Short=IF-3Mt;
DE Short=IF3(mt);
DE Short=IF3mt;
DE Flags: Precursor;
GN Name=MTIF3; ORFNames=DC38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 98-104, FUNCTION, AND
RP VARIANT LEU-243.
RC TISSUE=Melanocyte;
RX PubMed=12095986; DOI=10.1074/jbc.M202498200;
RA Koc E.C., Spremulli L.L.;
RT "Identification of mammalian mitochondrial translational initiation
RT factor 3 and examination of its role in initiation complex formation
RT with natural mRNAs.";
RL J. Biol. Chem. 277:35541-35549(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-243.
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RT "A novel gene from human dendritic cells.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-68 AND
RP LEU-243.
RC TISSUE=Cervix, and Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: IF-3 binds to the 28S ribosomal subunit and shifts the
CC equilibrum between 55S ribosomes and their 39S and 28S subunits in
CC favor of the free subunits, thus enhancing the availability of 28S
CC subunits on which protein synthesis initiation begins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- SIMILARITY: Belongs to the IF-3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39599.1; Type=Frameshift; Positions=246;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF410851; AAL04150.1; -; mRNA.
DR EMBL; AF265440; AAG44698.1; -; mRNA.
DR EMBL; AL137059; CAH70316.1; -; Genomic_DNA.
DR EMBL; BC039599; AAH39599.1; ALT_FRAME; mRNA.
DR EMBL; BC046166; AAH46166.1; -; mRNA.
DR RefSeq; NP_001159733.1; NM_001166261.1.
DR RefSeq; NP_001159734.1; NM_001166262.1.
DR RefSeq; NP_001159735.1; NM_001166263.1.
DR RefSeq; NP_690876.3; NM_152912.4.
DR RefSeq; XP_005266340.1; XM_005266283.1.
DR UniGene; Hs.534582; -.
DR ProteinModelPortal; Q9H2K0; -.
DR SMR; Q9H2K0; 149-250.
DR IntAct; Q9H2K0; 1.
DR STRING; 9606.ENSP00000370508; -.
DR DMDM; 74718093; -.
DR PaxDb; Q9H2K0; -.
DR PRIDE; Q9H2K0; -.
DR DNASU; 219402; -.
DR Ensembl; ENST00000381116; ENSP00000370508; ENSG00000122033.
DR Ensembl; ENST00000381120; ENSP00000370512; ENSG00000122033.
DR Ensembl; ENST00000405591; ENSP00000384659; ENSG00000122033.
DR Ensembl; ENST00000431572; ENSP00000400084; ENSG00000122033.
DR GeneID; 219402; -.
DR KEGG; hsa:219402; -.
DR UCSC; uc001urh.3; human.
DR CTD; 219402; -.
DR GeneCards; GC13M028009; -.
DR H-InvDB; HIX0011193; -.
DR HGNC; HGNC:29788; MTIF3.
DR HPA; HPA039791; -.
DR neXtProt; NX_Q9H2K0; -.
DR PharmGKB; PA162396264; -.
DR eggNOG; NOG87881; -.
DR HOGENOM; HOG000264227; -.
DR HOVERGEN; HBG080563; -.
DR InParanoid; Q9H2K0; -.
DR KO; K02520; -.
DR OMA; QTMPGIA; -.
DR OrthoDB; EOG7DZ8KV; -.
DR PhylomeDB; Q9H2K0; -.
DR ChiTaRS; MTIF3; human.
DR GenomeRNAi; 219402; -.
DR NextBio; 90583; -.
DR PRO; PR:Q9H2K0; -.
DR Bgee; Q9H2K0; -.
DR CleanEx; HS_MTIF3; -.
DR Genevestigator; Q9H2K0; -.
DR GO; GO:0005739; C:mitochondrion; IC:BHF-UCL.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:BHF-UCL.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; IDA:BHF-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001732; P:formation of translation initiation complex; IDA:BHF-UCL.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:BHF-UCL.
DR GO; GO:0032790; P:ribosome disassembly; IDA:BHF-UCL.
DR Gene3D; 3.10.20.80; -; 1.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019815; Translation_initiation_fac_3_C.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF00707; IF3_C; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
DR PROSITE; PS00938; IF3; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Initiation factor;
KW Mitochondrion; Polymorphism; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 31 Mitochondrion.
FT CHAIN 32 278 Translation initiation factor IF-3,
FT mitochondrial.
FT /FTId=PRO_0000280037.
FT VARIANT 68 68 T -> I (in dbSNP:rs17857314).
FT /FTId=VAR_031045.
FT VARIANT 243 243 F -> L (in dbSNP:rs1218825).
FT /FTId=VAR_031046.
SQ SEQUENCE 278 AA; 31725 MW; E0CA6D5F547DD6E3 CRC64;
MAALFLKRLT LQTVKSENSC IRCFGKHILQ KTAPAQLSPI ASAPRLSFLI HAKAFSTAED
TQNEGKKTKK NKTAFSNVGR KISQRVIHLF DEKGNDLGNM HRANVIRLMD ERDLRLVQRN
TSTEPAEYQL MTGLQILQER QRLREMEKAN PKTGPTLRKE LILSSNIGQH DLDTKTKQIQ
QWIKKKHLVQ ITIKKGKNVD VSENEMEEIF HQILQTMPGI ATFSSRPQAV QGGKALMCVL
RAFSKNEEKA YKETQETQER DTLNKDHGND KESNVLHQ
//
ID IF3M_HUMAN Reviewed; 278 AA.
AC Q9H2K0; Q05BL8; Q5W0V0; Q86X68;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 84.
DE RecName: Full=Translation initiation factor IF-3, mitochondrial;
DE Short=IF-3(Mt);
DE Short=IF-3Mt;
DE Short=IF3(mt);
DE Short=IF3mt;
DE Flags: Precursor;
GN Name=MTIF3; ORFNames=DC38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 98-104, FUNCTION, AND
RP VARIANT LEU-243.
RC TISSUE=Melanocyte;
RX PubMed=12095986; DOI=10.1074/jbc.M202498200;
RA Koc E.C., Spremulli L.L.;
RT "Identification of mammalian mitochondrial translational initiation
RT factor 3 and examination of its role in initiation complex formation
RT with natural mRNAs.";
RL J. Biol. Chem. 277:35541-35549(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-243.
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RT "A novel gene from human dendritic cells.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-68 AND
RP LEU-243.
RC TISSUE=Cervix, and Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: IF-3 binds to the 28S ribosomal subunit and shifts the
CC equilibrum between 55S ribosomes and their 39S and 28S subunits in
CC favor of the free subunits, thus enhancing the availability of 28S
CC subunits on which protein synthesis initiation begins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- SIMILARITY: Belongs to the IF-3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39599.1; Type=Frameshift; Positions=246;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF410851; AAL04150.1; -; mRNA.
DR EMBL; AF265440; AAG44698.1; -; mRNA.
DR EMBL; AL137059; CAH70316.1; -; Genomic_DNA.
DR EMBL; BC039599; AAH39599.1; ALT_FRAME; mRNA.
DR EMBL; BC046166; AAH46166.1; -; mRNA.
DR RefSeq; NP_001159733.1; NM_001166261.1.
DR RefSeq; NP_001159734.1; NM_001166262.1.
DR RefSeq; NP_001159735.1; NM_001166263.1.
DR RefSeq; NP_690876.3; NM_152912.4.
DR RefSeq; XP_005266340.1; XM_005266283.1.
DR UniGene; Hs.534582; -.
DR ProteinModelPortal; Q9H2K0; -.
DR SMR; Q9H2K0; 149-250.
DR IntAct; Q9H2K0; 1.
DR STRING; 9606.ENSP00000370508; -.
DR DMDM; 74718093; -.
DR PaxDb; Q9H2K0; -.
DR PRIDE; Q9H2K0; -.
DR DNASU; 219402; -.
DR Ensembl; ENST00000381116; ENSP00000370508; ENSG00000122033.
DR Ensembl; ENST00000381120; ENSP00000370512; ENSG00000122033.
DR Ensembl; ENST00000405591; ENSP00000384659; ENSG00000122033.
DR Ensembl; ENST00000431572; ENSP00000400084; ENSG00000122033.
DR GeneID; 219402; -.
DR KEGG; hsa:219402; -.
DR UCSC; uc001urh.3; human.
DR CTD; 219402; -.
DR GeneCards; GC13M028009; -.
DR H-InvDB; HIX0011193; -.
DR HGNC; HGNC:29788; MTIF3.
DR HPA; HPA039791; -.
DR neXtProt; NX_Q9H2K0; -.
DR PharmGKB; PA162396264; -.
DR eggNOG; NOG87881; -.
DR HOGENOM; HOG000264227; -.
DR HOVERGEN; HBG080563; -.
DR InParanoid; Q9H2K0; -.
DR KO; K02520; -.
DR OMA; QTMPGIA; -.
DR OrthoDB; EOG7DZ8KV; -.
DR PhylomeDB; Q9H2K0; -.
DR ChiTaRS; MTIF3; human.
DR GenomeRNAi; 219402; -.
DR NextBio; 90583; -.
DR PRO; PR:Q9H2K0; -.
DR Bgee; Q9H2K0; -.
DR CleanEx; HS_MTIF3; -.
DR Genevestigator; Q9H2K0; -.
DR GO; GO:0005739; C:mitochondrion; IC:BHF-UCL.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:BHF-UCL.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; IDA:BHF-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001732; P:formation of translation initiation complex; IDA:BHF-UCL.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:BHF-UCL.
DR GO; GO:0032790; P:ribosome disassembly; IDA:BHF-UCL.
DR Gene3D; 3.10.20.80; -; 1.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019815; Translation_initiation_fac_3_C.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF00707; IF3_C; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
DR PROSITE; PS00938; IF3; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Initiation factor;
KW Mitochondrion; Polymorphism; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 31 Mitochondrion.
FT CHAIN 32 278 Translation initiation factor IF-3,
FT mitochondrial.
FT /FTId=PRO_0000280037.
FT VARIANT 68 68 T -> I (in dbSNP:rs17857314).
FT /FTId=VAR_031045.
FT VARIANT 243 243 F -> L (in dbSNP:rs1218825).
FT /FTId=VAR_031046.
SQ SEQUENCE 278 AA; 31725 MW; E0CA6D5F547DD6E3 CRC64;
MAALFLKRLT LQTVKSENSC IRCFGKHILQ KTAPAQLSPI ASAPRLSFLI HAKAFSTAED
TQNEGKKTKK NKTAFSNVGR KISQRVIHLF DEKGNDLGNM HRANVIRLMD ERDLRLVQRN
TSTEPAEYQL MTGLQILQER QRLREMEKAN PKTGPTLRKE LILSSNIGQH DLDTKTKQIQ
QWIKKKHLVQ ITIKKGKNVD VSENEMEEIF HQILQTMPGI ATFSSRPQAV QGGKALMCVL
RAFSKNEEKA YKETQETQER DTLNKDHGND KESNVLHQ
//