T10B_MOUSE
ID T10B_MOUSE Reviewed; 100 AA.
AC Q9WV96; Q545D2; Q9DCB5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10 B;
DE AltName: Full=Mitochondrial import inner membrane translocase subunit Tim9 B;
DE AltName: Full=TIMM10B;
DE Short=Tim10b;
GN Name=Timm10b; Synonyms=Fxc1, Tim9b, Timm9b;
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=Brain, and Mammary gland;
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=129; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and Spleen;
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: Component of the TIM22 complex, a complex that mediates the
CC import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. The TIM22 complex forms a twin-pore
CC translocase that uses the membrane potential as the external driving
CC force. In the TIM22 complex, it may act as a docking point for the
CC soluble 70 kDa complex that guides the target proteins in transit
CC through the aqueous mitochondrial intermembrane space.
CC {ECO:0000250|UniProtKB:Q9Y5J6}.
CC -!- SUBUNIT: Component of the TIM22 complex, which core is composed of
CC TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and
CC TIMM29. {ECO:0000250|UniProtKB:Q9Y5J6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9Y5J6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y5J6}.
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 TIMM10B from cytoplasm into mitochondrion, the
CC Cys residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane.
CC {ECO:0000250|UniProtKB:P87108}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150103; AAD40009.1; -; mRNA.
DR EMBL; AK002949; BAB22474.1; -; mRNA.
DR EMBL; AK003368; BAB22742.1; -; mRNA.
DR EMBL; AK010994; BAB27313.1; -; mRNA.
DR EMBL; AK166190; BAE38620.1; -; mRNA.
DR EMBL; BC009158; AAH09158.1; -; mRNA.
DR CCDS; CCDS21657.1; -.
DR RefSeq; NP_062375.1; NM_019502.2.
DR RefSeq; XP_006507437.1; XM_006507374.3.
DR AlphaFoldDB; Q9WV96; -.
DR SMR; Q9WV96; -.
DR BioGRID; 199770; 5.
DR STRING; 10090.ENSMUSP00000102395; -.
DR PhosphoSitePlus; Q9WV96; -.
DR EPD; Q9WV96; -.
DR MaxQB; Q9WV96; -.
DR PaxDb; Q9WV96; -.
DR PeptideAtlas; Q9WV96; -.
DR PRIDE; Q9WV96; -.
DR DNASU; 14356; -.
DR Ensembl; ENSMUST00000058333; ENSMUSP00000057061; ENSMUSG00000089847.
DR Ensembl; ENSMUST00000106780; ENSMUSP00000102392; ENSMUSG00000089847.
DR Ensembl; ENSMUST00000106783; ENSMUSP00000102395; ENSMUSG00000089847.
DR Ensembl; ENSMUST00000142363; ENSMUSP00000148105; ENSMUSG00000110234.
DR Ensembl; ENSMUST00000142874; ENSMUSP00000147621; ENSMUSG00000110234.
DR Ensembl; ENSMUST00000211054; ENSMUSP00000148176; ENSMUSG00000110234.
DR GeneID; 14356; -.
DR KEGG; mmu:14356; -.
DR UCSC; uc009iys.1; mouse.
DR CTD; 26515; -.
DR MGI; MGI:1315196; Timm10b.
DR VEuPathDB; HostDB:ENSMUSG00000089847; -.
DR VEuPathDB; HostDB:ENSMUSG00000110234; -.
DR eggNOG; KOG3479; Eukaryota.
DR GeneTree; ENSGT00450000040326; -.
DR GeneTree; ENSGT00900000143782; -.
DR HOGENOM; CLU_141397_2_2_1; -.
DR InParanoid; Q9WV96; -.
DR OMA; CFNRCVD; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q9WV96; -.
DR TreeFam; TF106188; -.
DR BioGRID-ORCS; 14356; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Timm10b; mouse.
DR PRO; PR:Q9WV96; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9WV96; protein.
DR Bgee; ENSMUSG00000089847; Expressed in granulocyte and 199 other tissues.
DR ExpressionAtlas; Q9WV96; baseline and differential.
DR Genevisible; Q9WV96; 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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..100
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10 B"
FT /id="PRO_0000193599"
FT MOTIF 25..49
FT /note="Twin CX3C motif"
FT DISULFID 25..49
FT /evidence="ECO:0000250|UniProtKB:P87108"
FT DISULFID 29..45
FT /evidence="ECO:0000250|UniProtKB:P87108"
FT CONFLICT 37
FT /note="A -> V (in Ref. 2; BAB22474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 100 AA; 11314 MW; FB5BA31A60DA3858 CRC64;
MEQQQQQLRN LRDFLLVYNR MTELCFQRCV PSLHHRALDA EEEACLHSCA GKLIHSNHRL
MAAYVHLMPA LVQRRIADYE AASAAPGIPA EQTRDSPSGS
