IF3M_HUMAN
ID IF3M_HUMAN Reviewed; 278 AA.
AC Q9H2K0; Q05BL8; Q5W0V0; Q86X68;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 144.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 factor
RT 3 and examination of its role in initiation complex formation with natural
RT 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., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., 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., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., 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., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA 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 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 {ECO:0000269|PubMed:12095986}.
CC -!- INTERACTION:
CC Q9H2K0; P05090: APOD; NbExp=3; IntAct=EBI-3923617, EBI-715495;
CC Q9H2K0; Q07817: BCL2L1; NbExp=3; IntAct=EBI-3923617, EBI-78035;
CC Q9H2K0; O95393: BMP10; NbExp=3; IntAct=EBI-3923617, EBI-3922513;
CC Q9H2K0; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-3923617, EBI-953896;
CC Q9H2K0; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-3923617, EBI-12244618;
CC Q9H2K0; Q86V35: CABP7; NbExp=3; IntAct=EBI-3923617, EBI-23900553;
CC Q9H2K0; Q08722-3: CD47; NbExp=3; IntAct=EBI-3923617, EBI-17263290;
CC Q9H2K0; O14735: CDIPT; NbExp=3; IntAct=EBI-3923617, EBI-358858;
CC Q9H2K0; O95674: CDS2; NbExp=3; IntAct=EBI-3923617, EBI-3913685;
CC Q9H2K0; Q99675: CGRRF1; NbExp=3; IntAct=EBI-3923617, EBI-2130213;
CC Q9H2K0; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-3923617, EBI-11959453;
CC Q9H2K0; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-3923617, EBI-11989440;
CC Q9H2K0; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3923617, EBI-11522780;
CC Q9H2K0; P29400-2: COL4A5; NbExp=3; IntAct=EBI-3923617, EBI-12211159;
CC Q9H2K0; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-3923617, EBI-745535;
CC Q9H2K0; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-3923617, EBI-12019274;
CC Q9H2K0; Q07325: CXCL9; NbExp=3; IntAct=EBI-3923617, EBI-3911467;
CC Q9H2K0; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-3923617, EBI-2680384;
CC Q9H2K0; P78329: CYP4F2; NbExp=3; IntAct=EBI-3923617, EBI-1752413;
CC Q9H2K0; Q6UW88-2: EPGN; NbExp=3; IntAct=EBI-3923617, EBI-17468158;
CC Q9H2K0; Q9UGM5: FETUB; NbExp=3; IntAct=EBI-3923617, EBI-13049494;
CC Q9H2K0; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-3923617, EBI-12175685;
CC Q9H2K0; Q9UBD0: HSFX2; NbExp=3; IntAct=EBI-3923617, EBI-947253;
CC Q9H2K0; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-3923617, EBI-12937691;
CC Q9H2K0; P05107: ITGB2; NbExp=3; IntAct=EBI-3923617, EBI-300173;
CC Q9H2K0; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3923617, EBI-10266796;
CC Q9H2K0; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-3923617, EBI-3267258;
CC Q9H2K0; O43561-2: LAT; NbExp=3; IntAct=EBI-3923617, EBI-8070286;
CC Q9H2K0; P01130: LDLR; NbExp=3; IntAct=EBI-3923617, EBI-988319;
CC Q9H2K0; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3923617, EBI-2820517;
CC Q9H2K0; O14880: MGST3; NbExp=3; IntAct=EBI-3923617, EBI-724754;
CC Q9H2K0; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-3923617, EBI-995714;
CC Q9H2K0; P11836: MS4A1; NbExp=3; IntAct=EBI-3923617, EBI-2808234;
CC Q9H2K0; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-3923617, EBI-2863634;
CC Q9H2K0; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-3923617, EBI-11978907;
CC Q9H2K0; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-3923617, EBI-721750;
CC Q9H2K0; P26678: PLN; NbExp=3; IntAct=EBI-3923617, EBI-692836;
CC Q9H2K0; P60201-2: PLP1; NbExp=3; IntAct=EBI-3923617, EBI-12188331;
CC Q9H2K0; Q9NS64: RPRM; NbExp=3; IntAct=EBI-3923617, EBI-1052363;
CC Q9H2K0; O00767: SCD; NbExp=3; IntAct=EBI-3923617, EBI-2684237;
CC Q9H2K0; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-3923617, EBI-9679163;
CC Q9H2K0; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-3923617, EBI-10329948;
CC Q9H2K0; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-3923617, EBI-749270;
CC Q9H2K0; A2A2V5: SERTM1; NbExp=3; IntAct=EBI-3923617, EBI-17284533;
CC Q9H2K0; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-3923617, EBI-747107;
CC Q9H2K0; O60749: SNX2; NbExp=3; IntAct=EBI-3923617, EBI-1046690;
CC Q9H2K0; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-3923617, EBI-12023934;
CC Q9H2K0; Q96DR4: STARD4; NbExp=3; IntAct=EBI-3923617, EBI-17217258;
CC Q9H2K0; P02808: STATH; NbExp=3; IntAct=EBI-3923617, EBI-738687;
CC Q9H2K0; P0DN84: STRIT1; NbExp=3; IntAct=EBI-3923617, EBI-12200293;
CC Q9H2K0; Q13277: STX3; NbExp=3; IntAct=EBI-3923617, EBI-1394295;
CC Q9H2K0; O43752: STX6; NbExp=3; IntAct=EBI-3923617, EBI-2695795;
CC Q9H2K0; P07204: THBD; NbExp=3; IntAct=EBI-3923617, EBI-941422;
CC Q9H2K0; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-3923617, EBI-17192156;
CC Q9H2K0; Q6PL24: TMED8; NbExp=3; IntAct=EBI-3923617, EBI-11603430;
CC Q9H2K0; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-3923617, EBI-1057733;
CC Q9H2K0; P17152: TMEM11; NbExp=3; IntAct=EBI-3923617, EBI-723946;
CC Q9H2K0; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-3923617, EBI-10694905;
CC Q9H2K0; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-3923617, EBI-348587;
CC Q9H2K0; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-3923617, EBI-2800645;
CC Q9H2K0; A2RU14: TMEM218; NbExp=3; IntAct=EBI-3923617, EBI-10173151;
CC Q9H2K0; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-3923617, EBI-11528917;
CC Q9H2K0; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-3923617, EBI-10315004;
CC Q9H2K0; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-3923617, EBI-12887458;
CC Q9H2K0; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-3923617, EBI-11956809;
CC Q9H2K0; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-3923617, EBI-12038591;
CC Q9H2K0; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-3923617, EBI-12111910;
CC Q9H2K0; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-3923617, EBI-12045841;
CC Q9H2K0; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-3923617, EBI-12261790;
CC Q9H2K0; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-3923617, EBI-11988865;
CC Q9H2K0; Q53HI1: UNC50; NbExp=3; IntAct=EBI-3923617, EBI-7601760;
CC Q9H2K0; O75379: VAMP4; NbExp=3; IntAct=EBI-3923617, EBI-744953;
CC Q9H2K0; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-3923617, EBI-11337915;
CC Q9H2K0; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-3923617, EBI-751210;
CC Q9H2K0; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-3923617, EBI-12837904;
CC Q9H2K0; O95125: ZNF202; NbExp=3; IntAct=EBI-3923617, EBI-751960;
CC Q9H2K0; A0A087WZY1; NbExp=3; IntAct=EBI-3923617, EBI-13387614;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39599.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF410851; AAL04150.1; -; mRNA.
DR EMBL; AF265440; AAG44698.1; -; mRNA.
DR EMBL; AL137059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039599; AAH39599.1; ALT_FRAME; mRNA.
DR EMBL; BC046166; AAH46166.1; -; mRNA.
DR CCDS; CCDS9322.1; -.
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_006719834.1; XM_006719771.3.
DR RefSeq; XP_006719835.1; XM_006719772.3.
DR RefSeq; XP_011533259.1; XM_011534957.2.
DR RefSeq; XP_011533260.1; XM_011534958.2.
DR RefSeq; XP_011533261.1; XM_011534959.2.
DR RefSeq; XP_011533262.1; XM_011534960.2.
DR RefSeq; XP_011533263.1; XM_011534961.2.
DR RefSeq; XP_011533264.1; XM_011534962.2.
DR RefSeq; XP_011533265.1; XM_011534963.2.
DR RefSeq; XP_016875906.1; XM_017020417.1.
DR PDB; 6NEQ; EM; 3.32 A; z=32-278.
DR PDB; 6NF8; EM; 3.48 A; z=32-278.
DR PDB; 6RW4; EM; 2.97 A; 8=1-278.
DR PDB; 6RW5; EM; 3.14 A; 8=1-278.
DR PDBsum; 6NEQ; -.
DR PDBsum; 6NF8; -.
DR PDBsum; 6RW4; -.
DR PDBsum; 6RW5; -.
DR AlphaFoldDB; Q9H2K0; -.
DR SMR; Q9H2K0; -.
DR BioGRID; 128525; 289.
DR IntAct; Q9H2K0; 79.
DR STRING; 9606.ENSP00000370508; -.
DR iPTMnet; Q9H2K0; -.
DR PhosphoSitePlus; Q9H2K0; -.
DR BioMuta; MTIF3; -.
DR DMDM; 317373570; -.
DR EPD; Q9H2K0; -.
DR jPOST; Q9H2K0; -.
DR MassIVE; Q9H2K0; -.
DR MaxQB; Q9H2K0; -.
DR PaxDb; Q9H2K0; -.
DR PeptideAtlas; Q9H2K0; -.
DR PRIDE; Q9H2K0; -.
DR ProteomicsDB; 80558; -.
DR Antibodypedia; 22665; 320 antibodies from 26 providers.
DR DNASU; 219402; -.
DR Ensembl; ENST00000381116.5; ENSP00000370508.1; ENSG00000122033.15.
DR Ensembl; ENST00000381120.8; ENSP00000370512.3; ENSG00000122033.15.
DR Ensembl; ENST00000405591.3; ENSP00000384659.2; ENSG00000122033.15.
DR GeneID; 219402; -.
DR KEGG; hsa:219402; -.
DR MANE-Select; ENST00000381120.8; ENSP00000370512.3; NM_152912.5; NP_690876.3.
DR UCSC; uc001urh.4; human.
DR CTD; 219402; -.
DR DisGeNET; 219402; -.
DR GeneCards; MTIF3; -.
DR HGNC; HGNC:29788; MTIF3.
DR HPA; ENSG00000122033; Low tissue specificity.
DR MIM; 619554; gene.
DR neXtProt; NX_Q9H2K0; -.
DR OpenTargets; ENSG00000122033; -.
DR PharmGKB; PA162396264; -.
DR VEuPathDB; HostDB:ENSG00000122033; -.
DR eggNOG; ENOG502SBZS; Eukaryota.
DR GeneTree; ENSGT00390000014424; -.
DR HOGENOM; CLU_086230_0_1_1; -.
DR InParanoid; Q9H2K0; -.
DR OMA; SAGCVRW; -.
DR OrthoDB; 970215at2759; -.
DR PhylomeDB; Q9H2K0; -.
DR TreeFam; TF332326; -.
DR PathwayCommons; Q9H2K0; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR SignaLink; Q9H2K0; -.
DR BioGRID-ORCS; 219402; 25 hits in 1047 CRISPR screens.
DR ChiTaRS; MTIF3; human.
DR GenomeRNAi; 219402; -.
DR Pharos; Q9H2K0; Tbio.
DR PRO; PR:Q9H2K0; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9H2K0; protein.
DR Bgee; ENSG00000122033; Expressed in apex of heart and 186 other tissues.
DR Genevisible; Q9H2K0; HS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:BHF-UCL.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IDA:BHF-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0070124; P:mitochondrial translational initiation; IDA:SGD.
DR GO; GO:0032790; P:ribosome disassembly; IDA:BHF-UCL.
DR Gene3D; 3.10.20.80; -; 1.
DR Gene3D; 3.30.110.10; -; 1.
DR InterPro; IPR036788; T_IF-3_C_sf.
DR InterPro; IPR036787; T_IF-3_N_sf.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Initiation factor; Mitochondrion;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT CHAIN 32..278
FT /note="Translation initiation factor IF-3, mitochondrial"
FT /id="PRO_0000280037"
FT REGION 249..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 68
FT /note="T -> I (in dbSNP:rs17857314)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031045"
FT VARIANT 243
FT /note="F -> L (in dbSNP:rs1218825)"
FT /evidence="ECO:0000269|PubMed:12095986,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_031046"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:6NEQ"
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