TIM22_RAT
ID TIM22_RAT Reviewed; 192 AA.
AC Q9JKW1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim22;
GN Name=Timm22; Synonyms=Tim22;
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 3-192.
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).
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}.
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DR EMBL; AABR03073135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF223951; AAF28360.1; -; mRNA.
DR RefSeq; NP_116007.1; NM_032618.1.
DR AlphaFoldDB; Q9JKW1; -.
DR SMR; Q9JKW1; -.
DR STRING; 10116.ENSRNOP00000010779; -.
DR jPOST; Q9JKW1; -.
DR PaxDb; Q9JKW1; -.
DR PRIDE; Q9JKW1; -.
DR Ensembl; ENSRNOT00000010778; ENSRNOP00000010779; ENSRNOG00000007988.
DR GeneID; 79463; -.
DR KEGG; rno:79463; -.
DR CTD; 29928; -.
DR RGD; 68406; Timm22.
DR eggNOG; KOG3225; Eukaryota.
DR GeneTree; ENSGT00390000016067; -.
DR HOGENOM; CLU_091077_0_0_1; -.
DR InParanoid; Q9JKW1; -.
DR OMA; THSYAKN; -.
DR OrthoDB; 1544601at2759; -.
DR PhylomeDB; Q9JKW1; -.
DR PRO; PR:Q9JKW1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007988; Expressed in heart and 20 other tissues.
DR Genevisible; Q9JKW1; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
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:RGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:UniProtKB.
DR InterPro; IPR039175; TIM22.
DR PANTHER; PTHR14110; PTHR14110; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..192
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim22"
FT /id="PRO_0000228081"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 67..139
FT /evidence="ECO:0000250|UniProtKB:Q9Y584"
FT DISULFID 158..177
FT /evidence="ECO:0000250|UniProtKB:Q9Y584"
SQ SEQUENCE 192 AA; 19918 MW; 1BFA65ED3AF98A29 CRC64;
MAAAKAGASA PEAAGSAEAP LQYSLLLQHL VGDKRQPRLL EPGSLGGIPS PAKSEEQKMI
ERAMESCAFK AVLACVGGFV LGGAFGVFTA GIDTNVGFDP KDPYRTPTAR EVLKDMGQRG
MSYAKNFAIV GAMFSCTECL VESYRGKSDW KNSVISGCIT GGAIGFRAGV KAGAIGCGGF
AAFSAAIDYY LR
