TIM22_MOUSE
ID TIM22_MOUSE Reviewed; 194 AA.
AC Q9CQ85; Q5SSL1; Q5SSL2; Q8QZU2; Q9JKW2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim22;
GN Name=Timm22; Synonyms=Tim22;
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=Embryo;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Salivary 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Essential core component of the TIM22 complex, a complex that
CC mediates the import and insertion of multi-pass transmembrane proteins
CC into the mitochondrial inner membrane. In the TIM22 complex, it
CC constitutes the voltage-activated and signal-gated channel. Forms a
CC twin-pore translocase that uses the membrane potential as external
CC driving force in 2 voltage-dependent steps (By similarity).
CC {ECO:0000250|UniProtKB:Q12328}.
CC -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of
CC TIMM22, associated with peripheral protein FXC1/TIMM10B and the 70 kDa
CC heterohexamer. In most cases, the 70 kDa complex is composed of TIMM9
CC and TIMM10 (TIMM10A or TIMM10B). A small fraction of the 70 kDa complex
CC is composed of TIMM8 (TIMM8A/DDP1 or TIMM8B/DDP2) and TIMM13. The TIM22
CC complex also contains AGK and TIMM29. Interacts directly with TIMM9,
CC TIMM10A and FXC1/TIMM10B. Interacts (when oxidized) with TIMM29;
CC interaction is direct. {ECO:0000250|UniProtKB:Q9Y584}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9Y584}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Disulfide bonds promote efficient assembly of the TIM22 complex.
CC {ECO:0000250|UniProtKB:Q9Y584}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF223950; AAF28359.1; -; mRNA.
DR EMBL; AK012130; BAB28051.1; -; mRNA.
DR EMBL; AK017389; BAB30726.1; -; mRNA.
DR EMBL; AL663050; CAI25857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663050; CAI25858.1; -; Genomic_DNA.
DR EMBL; BC022610; AAH22610.1; -; mRNA.
DR EMBL; BC055279; AAH55279.1; -; mRNA.
DR CCDS; CCDS25065.1; -.
DR RefSeq; NP_001278090.1; NM_001291161.1.
DR RefSeq; NP_062792.2; NM_019818.5.
DR RefSeq; NP_075844.1; NM_023355.2.
DR AlphaFoldDB; Q9CQ85; -.
DR SMR; Q9CQ85; -.
DR IntAct; Q9CQ85; 1.
DR MINT; Q9CQ85; -.
DR STRING; 10090.ENSMUSP00000021203; -.
DR PhosphoSitePlus; Q9CQ85; -.
DR SwissPalm; Q9CQ85; -.
DR EPD; Q9CQ85; -.
DR jPOST; Q9CQ85; -.
DR MaxQB; Q9CQ85; -.
DR PaxDb; Q9CQ85; -.
DR PRIDE; Q9CQ85; -.
DR ProteomicsDB; 262785; -.
DR Antibodypedia; 22666; 29 antibodies from 15 providers.
DR DNASU; 56322; -.
DR Ensembl; ENSMUST00000021203; ENSMUSP00000021203; ENSMUSG00000020843.
DR GeneID; 56322; -.
DR KEGG; mmu:56322; -.
DR UCSC; uc007kfq.3; mouse.
DR CTD; 29928; -.
DR MGI; MGI:1929742; Timm22.
DR VEuPathDB; HostDB:ENSMUSG00000020843; -.
DR eggNOG; KOG3225; Eukaryota.
DR GeneTree; ENSGT00390000016067; -.
DR HOGENOM; CLU_091077_0_0_1; -.
DR InParanoid; Q9CQ85; -.
DR OMA; THSYAKN; -.
DR OrthoDB; 1544601at2759; -.
DR PhylomeDB; Q9CQ85; -.
DR TreeFam; TF105836; -.
DR BioGRID-ORCS; 56322; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Timm22; mouse.
DR PRO; PR:Q9CQ85; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQ85; protein.
DR Bgee; ENSMUSG00000020843; Expressed in morula and 257 other tissues.
DR ExpressionAtlas; Q9CQ85; baseline and differential.
DR Genevisible; Q9CQ85; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; 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:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140318; F:protein transporter activity; ISO:MGI.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:UniProtKB.
DR InterPro; IPR039175; TIM22.
DR PANTHER; PTHR14110; PTHR14110; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..194
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim22"
FT /id="PRO_0000210299"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 69..141
FT /evidence="ECO:0000250|UniProtKB:Q9Y584"
FT DISULFID 160..179
FT /evidence="ECO:0000250|UniProtKB:Q9Y584"
FT CONFLICT 38..39
FT /note="QP -> HA (in Ref. 1; AAF28359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 20114 MW; B3C3EC1FFE842CFD CRC64;
MAATAPKAGG SAPEAAGSAE APLQYSLLLQ YLVGDKRQPR LLEPGSLGGI PSPAKSEEQK
MIERAMESCA FKAVLACVGG FVLGGAFGIF TAGIDTNVGF DPKDPYRTPT AKEVLKDMGQ
RGMSYAKNFA IVGAMFSCTE CLVESYRGKS DWKNSVISGC ITGGAIGFRA GVKAGAIGCG
GFAAFSAAID YYLR
