ID   TIM9_RAT                Reviewed;          89 AA.
AC   Q9WV97;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN   Name=Timm9; Synonyms=Tim9, Tim9a, Timm9a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 46-89.
RA   Bauer M.F., Brunner M., Hofmann S.;
RT   "Cloning and mapping of the Tim10/DDP gene family encoding small zinc
RT   finger proteins involved in mitochondrial carrier import.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 24-34 AND 67-81, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
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; AABR03049301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF150102; AAD40008.1; ALT_TERM; mRNA.
DR   RefSeq; NP_001263358.1; NM_001276429.1.
DR   RefSeq; NP_001263359.1; NM_001276430.1.
DR   RefSeq; NP_598288.1; NM_133604.1.
DR   AlphaFoldDB; Q9WV97; -.
DR   SMR; Q9WV97; -.
DR   STRING; 10116.ENSRNOP00000010871; -.
DR   iPTMnet; Q9WV97; -.
DR   PhosphoSitePlus; Q9WV97; -.
DR   PaxDb; Q9WV97; -.
DR   PRIDE; Q9WV97; -.
DR   Ensembl; ENSRNOT00000010871; ENSRNOP00000010871; ENSRNOG00000008222.
DR   GeneID; 171139; -.
DR   KEGG; rno:171139; -.
DR   UCSC; RGD:621656; rat.
DR   CTD; 26520; -.
DR   RGD; 621656; Timm9.
DR   eggNOG; KOG3479; Eukaryota.
DR   GeneTree; ENSGT00940000160102; -.
DR   HOGENOM; CLU_141397_3_3_1; -.
DR   InParanoid; Q9WV97; -.
DR   OMA; QDFLRMY; -.
DR   OrthoDB; 1627953at2759; -.
DR   PhylomeDB; Q9WV97; -.
DR   TreeFam; TF106192; -.
DR   PRO; PR:Q9WV97; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000008222; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q9WV97; RN.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISO:RGD.
DR   GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISO:RGD.
DR   GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR   GO; GO:0032977; F:membrane insertase activity; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISO:RGD.
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_0000193597"
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"
FT   CONFLICT        67..68
FT                   /note="FQ -> E (in Ref. 2; AAD40008)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="A -> V (in Ref. 2; AAD40008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  10376 MW;  00F17CF491A09548 CRC64;
     MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEEVTCSE HCLQKYLKMT
     QRISMRFQEY HIQQNEALAA KAGLLGQPR