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IF3M_MOUSE
ID   IF3M_MOUSE              Reviewed;         276 AA.
AC   Q9CZD5; Q14BP1; Q14BP2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
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;
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].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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   [2]
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   [3]
RP   STRUCTURE BY NMR OF 148-246.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of C-terminal domain of Riken cDNA 2810012L14.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000305}.
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DR   EMBL; AK012733; BAB28438.1; -; mRNA.
DR   EMBL; AK147090; BAE27670.1; -; mRNA.
DR   EMBL; BC115684; AAI15685.1; -; mRNA.
DR   EMBL; BC115685; AAI15686.1; -; mRNA.
DR   CCDS; CCDS19874.1; -.
DR   RefSeq; NP_001243029.1; NM_001256100.1.
DR   RefSeq; NP_001243030.1; NM_001256101.1.
DR   RefSeq; NP_001243031.1; NM_001256102.1.
DR   RefSeq; NP_083857.1; NM_029581.4.
DR   RefSeq; XP_006504952.1; XM_006504889.3.
DR   PDB; 2CRQ; NMR; -; A=148-246.
DR   PDBsum; 2CRQ; -.
DR   AlphaFoldDB; Q9CZD5; -.
DR   SMR; Q9CZD5; -.
DR   STRING; 10090.ENSMUSP00000063398; -.
DR   PhosphoSitePlus; Q9CZD5; -.
DR   MaxQB; Q9CZD5; -.
DR   PaxDb; Q9CZD5; -.
DR   PRIDE; Q9CZD5; -.
DR   ProteomicsDB; 273094; -.
DR   Antibodypedia; 22665; 320 antibodies from 26 providers.
DR   DNASU; 76366; -.
DR   Ensembl; ENSMUST00000016654; ENSMUSP00000016654; ENSMUSG00000016510.
DR   Ensembl; ENSMUST00000066675; ENSMUSP00000063398; ENSMUSG00000016510.
DR   Ensembl; ENSMUST00000110564; ENSMUSP00000106193; ENSMUSG00000016510.
DR   Ensembl; ENSMUST00000110566; ENSMUSP00000106195; ENSMUSG00000016510.
DR   GeneID; 76366; -.
DR   KEGG; mmu:76366; -.
DR   UCSC; uc009anp.2; mouse.
DR   CTD; 219402; -.
DR   MGI; MGI:1923616; Mtif3.
DR   VEuPathDB; HostDB:ENSMUSG00000016510; -.
DR   eggNOG; ENOG502SBZS; Eukaryota.
DR   GeneTree; ENSGT00390000014424; -.
DR   HOGENOM; CLU_086230_0_1_1; -.
DR   InParanoid; Q9CZD5; -.
DR   OMA; SAGCVRW; -.
DR   OrthoDB; 970215at2759; -.
DR   PhylomeDB; Q9CZD5; -.
DR   TreeFam; TF332326; -.
DR   BioGRID-ORCS; 76366; 8 hits in 71 CRISPR screens.
DR   ChiTaRS; Mtif3; mouse.
DR   EvolutionaryTrace; Q9CZD5; -.
DR   PRO; PR:Q9CZD5; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9CZD5; protein.
DR   Bgee; ENSMUSG00000016510; Expressed in animal zygote and 145 other tissues.
DR   ExpressionAtlas; Q9CZD5; baseline and differential.
DR   Genevisible; Q9CZD5; MM.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0043024; F:ribosomal small subunit binding; ISS:HGNC.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0008135; F:translation factor activity, RNA binding; ISS:HGNC.
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:HGNC.
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; 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   TIGRFAMs; TIGR00168; infC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Initiation factor; Mitochondrion; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   PROPEP          32..94
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000280038"
FT   CHAIN           95..276
FT                   /note="Translation initiation factor IF-3, mitochondrial"
FT                   /id="PRO_0000280039"
FT   REGION          244..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        34
FT                   /note="A -> T (in Ref. 2; AAI15686)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="R -> I (in Ref. 2; AAI15685)"
FT                   /evidence="ECO:0000305"
FT   STRAND          155..161
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   HELIX           166..181
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   STRAND          185..191
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   HELIX           200..211
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   STRAND          219..227
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:2CRQ"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:2CRQ"
SQ   SEQUENCE   276 AA;  31739 MW;  1D1D533F045F5AFE CRC64;
     MAVLLMRLML QTTKLDHNLI GRCLQRHAVK PDPAQLSLSA STPKLLYLTS AKGFSTAGDP
     QGERKQKRRD AFSNTGRKIS ERIIRVLDEK GMDLGMMHRA DVIRLMNKQD LRLVQRNTSS
     EPPEYQLMTG EQIHQERLKL REQEKAKPKT GPTMTKELVF SSNIGQHDLD TKSKQIQQWI
     EKKYHVQVTI KRRKDAEQSE EETEEIFNQI LQTMPDIATF SSRPKAIRGG TASMCVFRHL
     SKKEEKAYRE SQESQRRDTL SKDDDGNSKE SDVVCQ
 
 
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