TIM9_MOUSE
ID TIM9_MOUSE Reviewed; 89 AA.
AC Q9WV98;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN Name=Timm9; Synonyms=Tim9, Tim9a, Timm9a;
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 [MRNA].
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP PROTEIN SEQUENCE OF 16-34 AND 67-89, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. May also be required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of
CC TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-
CC bladed alpha-propeller structure and associates with the TIMM22
CC component of the TIM22 complex. Interacts with multi-pass transmembrane
CC proteins in transit. Also forms a complex composed of TIMM9,
CC TIMM10/TIM10A and FXC1/TIM10B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIMM9 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150101; AAD40007.1; -; mRNA.
DR EMBL; AK018764; BAB31394.1; -; mRNA.
DR EMBL; BC024370; AAH24370.1; -; mRNA.
DR CCDS; CCDS25962.1; -.
DR PIR; T51192; T51192.
DR RefSeq; NP_001020024.1; NM_001024853.1.
DR RefSeq; NP_001020025.1; NM_001024854.1.
DR RefSeq; NP_001273132.1; NM_001286203.2.
DR RefSeq; NP_038924.1; NM_013896.3.
DR RefSeq; XP_011242424.1; XM_011244122.2.
DR RefSeq; XP_017170577.1; XM_017315088.1.
DR AlphaFoldDB; Q9WV98; -.
DR SMR; Q9WV98; -.
DR BioGRID; 205958; 5.
DR IntAct; Q9WV98; 1.
DR STRING; 10090.ENSMUSP00000126298; -.
DR PhosphoSitePlus; Q9WV98; -.
DR EPD; Q9WV98; -.
DR jPOST; Q9WV98; -.
DR MaxQB; Q9WV98; -.
DR PaxDb; Q9WV98; -.
DR PeptideAtlas; Q9WV98; -.
DR PRIDE; Q9WV98; -.
DR ProteomicsDB; 262788; -.
DR Antibodypedia; 116; 119 antibodies from 22 providers.
DR DNASU; 30056; -.
DR Ensembl; ENSMUST00000021486; ENSMUSP00000021486; ENSMUSG00000021079.
DR Ensembl; ENSMUST00000166120; ENSMUSP00000126298; ENSMUSG00000021079.
DR Ensembl; ENSMUST00000220482; ENSMUSP00000152114; ENSMUSG00000021079.
DR Ensembl; ENSMUST00000221367; ENSMUSP00000152574; ENSMUSG00000021079.
DR Ensembl; ENSMUST00000221559; ENSMUSP00000152455; ENSMUSG00000021079.
DR GeneID; 30056; -.
DR KEGG; mmu:30056; -.
DR UCSC; uc007nuh.1; mouse.
DR CTD; 26520; -.
DR MGI; MGI:1353436; Timm9.
DR VEuPathDB; HostDB:ENSMUSG00000021079; -.
DR eggNOG; KOG3479; Eukaryota.
DR GeneTree; ENSGT00940000160102; -.
DR HOGENOM; CLU_141397_3_3_1; -.
DR InParanoid; Q9WV98; -.
DR OMA; QDFLRMY; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q9WV98; -.
DR TreeFam; TF106192; -.
DR BioGRID-ORCS; 30056; 10 hits in 70 CRISPR screens.
DR ChiTaRS; Timm9; mouse.
DR PRO; PR:Q9WV98; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WV98; protein.
DR Bgee; ENSMUSG00000021079; Expressed in ectoplacental cone and 277 other tissues.
DR ExpressionAtlas; Q9WV98; baseline and differential.
DR Genevisible; Q9WV98; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0032977; F:membrane insertase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:BHF-UCL.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Direct protein sequencing; Disulfide bond;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J7"
FT CHAIN 2..89
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim9"
FT /id="PRO_0000193596"
FT MOTIF 28..52
FT /note="Twin CX3C motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J7"
FT DISULFID 28..52
FT /evidence="ECO:0000250"
FT DISULFID 32..48
FT /evidence="ECO:0000250"
SQ SEQUENCE 89 AA; 10344 MW; 1A40D7F491A09548 CRC64;
MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEEVTCSE HCLQKYLKMT
QRISVRFQEY HIQQNEALAA KAGLLGQPR
