TIM13_MOUSE
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 03-AUG-2022, entry version 143.
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, 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).
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; 2.
DR MINT; P62075; -.
DR STRING; 10090.ENSMUSP00000020440; -.
DR iPTMnet; P62075; -.
DR PhosphoSitePlus; P62075; -.
DR EPD; P62075; -.
DR jPOST; P62075; -.
DR MaxQB; P62075; -.
DR PaxDb; P62075; -.
DR PeptideAtlas; P62075; -.
DR PRIDE; P62075; -.
DR ProteomicsDB; 259452; -.
DR Antibodypedia; 23013; 52 antibodies from 18 providers.
DR DNASU; 30055; -.
DR Ensembl; ENSMUST00000020440; ENSMUSP00000020440; ENSMUSG00000020219.
DR GeneID; 30055; -.
DR KEGG; mmu:30055; -.
DR UCSC; uc007gfi.2; mouse.
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; 1566384at2759; -.
DR PhylomeDB; P62075; -.
DR TreeFam; TF106194; -.
DR BioGRID-ORCS; 30055; 29 hits in 76 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 69 other tissues.
DR ExpressionAtlas; P62075; baseline and differential.
DR Genevisible; P62075; MM.
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; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR InterPro; IPR039238; Tim8/13.
DR PANTHER; PTHR19338; PTHR19338; 1.
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 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
