ID   TIM13_MOUSE             Reviewed;          95 AA.
AC   P62075; Q91VM6; Q9DC89; Q9UHL8; Q9WTL1;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13;
GN   Name=Timm13; Synonyms=Tim13a, Timm13a;
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, and NOD; TISSUE=Brain, Thymus, and Tongue;
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   TISSUE=Mammary tumor;
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 28-41 AND 50-64, 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   TISSUE SPECIFICITY.
RX   PubMed=15254020; DOI=10.1093/hmg/ddh217;
RA   Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.;
RT   "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are
RT   new substrates for the DDP1/TIMM8a-TIMM13 complex.";
RL   Hum. Mol. Genet. 13:2101-2111(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
RN   [7]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of some multi-pass transmembrane proteins into
CC       the mitochondrial inner membrane. Also 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. The TIMM8-
CC       TIMM13 complex mediates the import of proteins such as TIMM23,
CC       SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-
CC       TIMM10 70 kDa complex mediates the import of much more proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or
CC       TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex.
CC       Associates with the TIM22 complex, whose core is composed of TIMM22 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Present at high level in liver and brain, and at
CC       lower level in muscle and heart. In CNS sections, it is predominantly
CC       present in the soma and the dendritic portion of the Purkinje cells of
CC       the cerebellum, but not in the glial cells. Scattered expression also
CC       is also detected in the brain stem, olfactory bulb, substantia nigra,
CC       hippocampus and striatum (at protein level).
CC       {ECO:0000269|PubMed:15254020}.
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 TIMM13 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; AF144702; AAD39953.1; -; mRNA.
DR   EMBL; AK003054; BAB22536.1; -; mRNA.
DR   EMBL; AK009041; BAB26042.1; -; mRNA.
DR   EMBL; AK009152; BAB26109.1; -; mRNA.
DR   EMBL; AK013230; BAB28728.1; -; mRNA.
DR   EMBL; AK088984; BAC40687.1; -; mRNA.
DR   EMBL; BC011436; AAH11436.1; -; mRNA.
DR   CCDS; CCDS35989.1; -.
DR   RefSeq; NP_038923.1; NM_013895.4.
DR   AlphaFoldDB; P62075; -.
DR   SMR; P62075; -.
DR   BioGRID; 205957; 8.
DR   IntAct; P62075; 3.
DR   MINT; P62075; -.
DR   STRING; 10090.ENSMUSP00000020440; -.
DR   iPTMnet; P62075; -.
DR   PhosphoSitePlus; P62075; -.
DR   SwissPalm; P62075; -.
DR   EPD; P62075; -.
DR   jPOST; P62075; -.
DR   MaxQB; P62075; -.
DR   PaxDb; 10090-ENSMUSP00000020440; -.
DR   PeptideAtlas; P62075; -.
DR   ProteomicsDB; 259452; -.
DR   Pumba; P62075; -.
DR   Antibodypedia; 23013; 55 antibodies from 18 providers.
DR   DNASU; 30055; -.
DR   Ensembl; ENSMUST00000020440.7; ENSMUSP00000020440.7; ENSMUSG00000020219.8.
DR   GeneID; 30055; -.
DR   KEGG; mmu:30055; -.
DR   UCSC; uc007gfi.2; mouse.
DR   AGR; MGI:1353432; -.
DR   CTD; 26517; -.
DR   MGI; MGI:1353432; Timm13.
DR   VEuPathDB; HostDB:ENSMUSG00000020219; -.
DR   eggNOG; KOG1733; Eukaryota.
DR   GeneTree; ENSGT00390000014000; -.
DR   HOGENOM; CLU_141397_0_2_1; -.
DR   InParanoid; P62075; -.
DR   OMA; MAAWNQV; -.
DR   OrthoDB; 226619at2759; -.
DR   PhylomeDB; P62075; -.
DR   TreeFam; TF106194; -.
DR   BioGRID-ORCS; 30055; 29 hits in 81 CRISPR screens.
DR   ChiTaRS; Timm13; mouse.
DR   PRO; PR:P62075; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P62075; Protein.
DR   Bgee; ENSMUSG00000020219; Expressed in yolk sac and 71 other cell types or tissues.
DR   ExpressionAtlas; P62075; baseline and differential.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
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   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; Tim10-like; 1.
DR   Genevisible; P62075; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Direct protein sequencing; Disulfide bond;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW   Transport; Zinc.
FT   CHAIN           1..95
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim13"
FT                   /id="PRO_0000193624"
FT   MOTIF           46..69
FT                   /note="Twin CX3C motif"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5L4"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5L4"
FT   MOD_RES         53
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   DISULFID        46..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..65
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3
FT                   /note="S -> G (in Ref. 2; BAB22536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="D -> S (in Ref. 3; AAH11436)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   95 AA;  10458 MW;  F9A50A2E7F6E64C8 CRC64;
     MDSGFGSDFG GTGGGKLDPG AIMEQVKVQI AVANAQELLQ RMTDKCFRKC IGKPGGSLDN
     SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM
//