ID   TIM9_HUMAN              Reviewed;          89 AA.
AC   Q9Y5J7; B2R584;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN   Name=TIMM9; Synonyms=TIM9, TIM9A, TIMM9A;
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], AND TISSUE SPECIFICITY.
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10552927; DOI=10.1006/geno.1999.5966;
RA   Jin H., Kendall E., Freeman T.C., Roberts R.G., Vetrie D.L.P.;
RT   "The human family of deafness/dystonia peptide (DDP) related mitochondrial
RT   import proteins.";
RL   Genomics 61:259-267(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta, and Skin;
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   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11489896; DOI=10.1074/jbc.m105313200;
RA   Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D.,
RA   Neupert W., Brunner M., Bauer M.F.;
RT   "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23
RT   into the inner membrane of mitochondria.";
RL   J. Biol. Chem. 276:37327-37334(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIMM10; TIMM22 AND
RP   FXC1.
RX   PubMed=14726512; DOI=10.1074/jbc.m312485200;
RA   Muehlenbein N., Hofmann S., Rothbauer U., Bauer M.F.;
RT   "Organization and function of the small Tim complexes acting along the
RT   import pathway of metabolite carriers into mammalian mitochondria.";
RL   J. Biol. Chem. 279:13540-13546(2004).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
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).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH TIMM10, AND DISULFIDE
RP   BONDS.
RX   PubMed=16387659; DOI=10.1016/j.molcel.2005.11.010;
RA   Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., Gulbis J.M.;
RT   "Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-
RT   bladed alpha-propeller.";
RL   Mol. Cell 21:123-133(2006).
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.
CC       {ECO:0000269|PubMed:14726512}.
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. {ECO:0000269|PubMed:14726512,
CC       ECO:0000269|PubMed:16387659}.
CC   -!- INTERACTION:
CC       Q9Y5J7; P62072: TIMM10; NbExp=5; IntAct=EBI-1200370, EBI-1200391;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:11489896,
CC       ECO:0000269|PubMed:14726512}; Intermembrane side
CC       {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC       kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10552927,
CC       ECO:0000269|PubMed:10611480}.
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 (Probable).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR   EMBL; AF150100; AAD40006.1; -; mRNA.
DR   EMBL; AF152353; AAF15103.1; -; mRNA.
DR   EMBL; AK312095; BAG35031.1; -; mRNA.
DR   EMBL; CH471061; EAW80735.1; -; Genomic_DNA.
DR   EMBL; BC020213; AAH20213.1; -; mRNA.
DR   EMBL; BC054875; AAH54875.1; -; mRNA.
DR   CCDS; CCDS9735.1; -.
DR   PIR; T51191; T51191.
DR   RefSeq; NP_001291414.1; NM_001304485.1.
DR   RefSeq; NP_001291415.1; NM_001304486.1.
DR   RefSeq; NP_001291416.1; NM_001304487.1.
DR   RefSeq; NP_001291417.1; NM_001304488.1.
DR   RefSeq; NP_001291418.1; NM_001304489.1.
DR   RefSeq; NP_001291419.1; NM_001304490.1.
DR   RefSeq; NP_001291420.1; NM_001304491.1.
DR   RefSeq; NP_036592.1; NM_012460.3.
DR   PDB; 2BSK; X-ray; 3.30 A; A/C/E=1-89.
DR   PDB; 7CGP; EM; 3.70 A; D/E/F/K/L=1-89.
DR   PDBsum; 2BSK; -.
DR   PDBsum; 7CGP; -.
DR   AlphaFoldDB; Q9Y5J7; -.
DR   SMR; Q9Y5J7; -.
DR   BioGRID; 117724; 50.
DR   ComplexPortal; CPX-6124; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR   ComplexPortal; CPX-6125; TIM9-TIM10 mitochondrial intermembrane space protein transporter complex.
DR   ComplexPortal; CPX-6126; TIM9-TIM10-TIM10B mitochondrial intermembrane space protein transporter complex.
DR   CORUM; Q9Y5J7; -.
DR   IntAct; Q9Y5J7; 16.
DR   MINT; Q9Y5J7; -.
DR   STRING; 9606.ENSP00000378588; -.
DR   iPTMnet; Q9Y5J7; -.
DR   PhosphoSitePlus; Q9Y5J7; -.
DR   BioMuta; TIMM9; -.
DR   EPD; Q9Y5J7; -.
DR   jPOST; Q9Y5J7; -.
DR   MassIVE; Q9Y5J7; -.
DR   MaxQB; Q9Y5J7; -.
DR   PaxDb; 9606-ENSP00000378588; -.
DR   PeptideAtlas; Q9Y5J7; -.
DR   ProteomicsDB; 86422; -.
DR   Pumba; Q9Y5J7; -.
DR   Antibodypedia; 116; 136 antibodies from 22 providers.
DR   DNASU; 26520; -.
DR   Ensembl; ENST00000395159.7; ENSP00000378588.2; ENSG00000100575.14.
DR   Ensembl; ENST00000555061.5; ENSP00000450638.1; ENSG00000100575.14.
DR   Ensembl; ENST00000555404.5; ENSP00000451198.1; ENSG00000100575.14.
DR   Ensembl; ENST00000555593.5; ENSP00000451006.1; ENSG00000100575.14.
DR   GeneID; 26520; -.
DR   KEGG; hsa:26520; -.
DR   MANE-Select; ENST00000395159.7; ENSP00000378588.2; NM_012460.4; NP_036592.1.
DR   UCSC; uc001xds.4; human.
DR   AGR; HGNC:11819; -.
DR   CTD; 26520; -.
DR   DisGeNET; 26520; -.
DR   GeneCards; TIMM9; -.
DR   HGNC; HGNC:11819; TIMM9.
DR   HPA; ENSG00000100575; Low tissue specificity.
DR   MIM; 607384; gene.
DR   neXtProt; NX_Q9Y5J7; -.
DR   OpenTargets; ENSG00000100575; -.
DR   PharmGKB; PA36525; -.
DR   VEuPathDB; HostDB:ENSG00000100575; -.
DR   eggNOG; KOG3479; Eukaryota.
DR   GeneTree; ENSGT00940000160102; -.
DR   HOGENOM; CLU_141397_3_3_1; -.
DR   InParanoid; Q9Y5J7; -.
DR   OMA; QDFLRMY; -.
DR   OrthoDB; 8465at2759; -.
DR   PhylomeDB; Q9Y5J7; -.
DR   TreeFam; TF106192; -.
DR   PathwayCommons; Q9Y5J7; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   SignaLink; Q9Y5J7; -.
DR   SIGNOR; Q9Y5J7; -.
DR   BioGRID-ORCS; 26520; 506 hits in 1144 CRISPR screens.
DR   ChiTaRS; TIMM9; human.
DR   EvolutionaryTrace; Q9Y5J7; -.
DR   GeneWiki; TIMM9; -.
DR   GenomeRNAi; 26520; -.
DR   Pharos; Q9Y5J7; Tbio.
DR   PRO; PR:Q9Y5J7; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y5J7; Protein.
DR   Bgee; ENSG00000100575; Expressed in body of pancreas and 199 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5J7; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:BHF-UCL.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ComplexPortal.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IPI:ComplexPortal.
DR   GO; GO:0032977; F:membrane insertase activity; IDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:BHF-UCL.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; TAS:ProtInc.
DR   GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR   Gene3D; 1.10.287.810; Mitochondrial import inner membrane translocase subunit tim13 like domains; 1.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   PANTHER; PTHR13172:SF5; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM9; 1.
DR   PANTHER; PTHR13172; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM9B; 1.
DR   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; Tim10-like; 1.
DR   Genevisible; Q9Y5J7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Disulfide bond; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..89
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim9"
FT                   /id="PRO_0000193595"
FT   MOTIF           28..52
FT                   /note="Twin CX3C motif"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   DISULFID        28..52
FT                   /evidence="ECO:0000269|PubMed:16387659"
FT   DISULFID        32..48
FT                   /evidence="ECO:0000269|PubMed:16387659"
FT   HELIX           15..32
FT                   /evidence="ECO:0007829|PDB:2BSK"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:2BSK"
FT   HELIX           43..71
FT                   /evidence="ECO:0007829|PDB:2BSK"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:2BSK"
FT   HELIX           76..81
FT                   /evidence="ECO:0007829|PDB:2BSK"
SQ   SEQUENCE   89 AA;  10378 MW;  00F17CF6332ABF48 CRC64;
     MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEETTCSE HCLQKYLKMT
     QRISMRFQEY HIQQNEALAA KAGLLGQPR
//