TI172_ARATH
ID TI172_ARATH Reviewed; 243 AA.
AC Q9SP35; Q9ZUS5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM17-2;
GN Name=TIM17-2; OrderedLocusNames=At2g37410; ORFNames=F3G5.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miernyk J.A., Coop N.E.;
RT "A component of the Arabidopsis thaliana mitochondrial inner membrane
RT protein translocase, atTIM17.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12692332; DOI=10.1104/pp.102.016808;
RA Murcha M.W., Lister R., Ho A.Y., Whelan J.;
RT "Identification, expression, and import of components 17 and 23 of the
RT inner mitochondrial membrane translocase from Arabidopsis.";
RL Plant Physiol. 131:1737-1747(2003).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INDUCTION.
RX PubMed=14730085; DOI=10.1104/pp.103.033910;
RA Lister R., Chew O., Lee M.N., Heazlewood J.L., Clifton R., Parker K.L.,
RA Millar A.H., Whelan J.;
RT "A transcriptomic and proteomic characterization of the Arabidopsis
RT mitochondrial protein import apparatus and its response to mitochondrial
RT dysfunction.";
RL Plant Physiol. 134:777-789(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15722347; DOI=10.1074/jbc.m413299200;
RA Murcha M.W., Elhafez D., Millar A.H., Whelan J.;
RT "The C-terminal region of TIM17 links the outer and inner mitochondrial
RT membranes in Arabidopsis and is essential for protein import.";
RL J. Biol. Chem. 280:16476-16483(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17098851; DOI=10.1104/pp.106.090688;
RA Murcha M.W., Elhafez D., Lister R., Tonti-Filippini J., Baumgartner M.,
RA Philippar K., Carrie C., Mokranjac D., Soll J., Whelan J.;
RT "Characterization of the preprotein and amino acid transporter gene family
RT in Arabidopsis.";
RL Plant Physiol. 143:199-212(2007).
RN [9]
RP INTERACTION WITH TIM23-2, AND DISRUPTION PHENOTYPE.
RX PubMed=22730406; DOI=10.1105/tpc.112.098731;
RA Wang Y., Carrie C., Giraud E., Elhafez D., Narsai R., Duncan O., Whelan J.,
RA Murcha M.W.;
RT "Dual location of the mitochondrial preprotein transporters B14.7 and
RT Tim23-2 in complex I and the TIM17:23 complex in Arabidopsis links
RT mitochondrial activity and biogenesis.";
RL Plant Cell 24:2675-2695(2012).
CC -!- FUNCTION: Essential component of the TIM17:23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. Links the inner and outer
CC membranes. {ECO:0000269|PubMed:12692332, ECO:0000269|PubMed:15722347}.
CC -!- SUBUNIT: Component of the TIM17:23 complex at least composed of TIM23,
CC TIM17 and TIM50. The complex interacts with the TIM44 component of the
CC PAM complex (By similarity). Interacts with TIM23-2. {ECO:0000250,
CC ECO:0000269|PubMed:22730406}.
CC -!- INTERACTION:
CC Q9SP35; Q9SZU7: KAI2; NbExp=5; IntAct=EBI-25529919, EBI-25519488;
CC Q9SP35; Q9SIM9: MAX2; NbExp=3; IntAct=EBI-25529919, EBI-25529872;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12692332, ECO:0000269|PubMed:14730085,
CC ECO:0000269|PubMed:15722347, ECO:0000269|PubMed:17098851}. Note=The C-
CC terminal region is located in the outer membrane.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, leaves and young
CC cotyledons. {ECO:0000269|PubMed:12692332, ECO:0000269|PubMed:14730085}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression during cotyledon development.
CC {ECO:0000269|PubMed:12692332}.
CC -!- INDUCTION: Up-regulated after antimycin A or rotenone treatments.
CC {ECO:0000269|PubMed:14730085}.
CC -!- DOMAIN: An internal targeting signal (103-117) is required for
CC insertion into the mitochondrial inner membrane in a membrane
CC potential-dependent manner. The C-terminal region is exposed on the
CC outer surface of the outer membrane and is essential for protein
CC import.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:22730406}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR EMBL; AF186847; AAF03749.1; -; mRNA.
DR EMBL; AC005896; AAC98060.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09394.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09395.1; -; Genomic_DNA.
DR EMBL; AF360258; AAK25968.1; -; mRNA.
DR EMBL; AY040072; AAK64130.1; -; mRNA.
DR EMBL; AY056107; AAL06994.1; -; mRNA.
DR PIR; D84792; D84792.
DR RefSeq; NP_181277.1; NM_129296.4.
DR RefSeq; NP_973621.1; NM_201892.1.
DR AlphaFoldDB; Q9SP35; -.
DR BioGRID; 3661; 3.
DR IntAct; Q9SP35; 2.
DR STRING; 3702.AT2G37410.1; -.
DR TCDB; 3.A.8.1.4; the mitochondrial protein translocase (mpt) family.
DR PaxDb; Q9SP35; -.
DR PRIDE; Q9SP35; -.
DR ProteomicsDB; 234398; -.
DR EnsemblPlants; AT2G37410.1; AT2G37410.1; AT2G37410.
DR EnsemblPlants; AT2G37410.2; AT2G37410.2; AT2G37410.
DR GeneID; 818317; -.
DR Gramene; AT2G37410.1; AT2G37410.1; AT2G37410.
DR Gramene; AT2G37410.2; AT2G37410.2; AT2G37410.
DR KEGG; ath:AT2G37410; -.
DR Araport; AT2G37410; -.
DR TAIR; locus:2049771; AT2G37410.
DR eggNOG; KOG1652; Eukaryota.
DR HOGENOM; CLU_087811_0_0_1; -.
DR InParanoid; Q9SP35; -.
DR OMA; MGQVPGM; -.
DR OrthoDB; 1590221at2759; -.
DR PhylomeDB; Q9SP35; -.
DR PRO; PR:Q9SP35; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SP35; baseline and differential.
DR Genevisible; Q9SP35; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:TAIR.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Protein transport; Reference proteome;
KW Repeat; Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..243
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM17-2"
FT /id="PRO_0000210293"
FT TRANSMEM 19..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 149..151
FT /note="1"
FT REPEAT 152..154
FT /note="2"
FT REPEAT 155..157
FT /note="3"
FT REPEAT 158..160
FT /note="4"
FT REPEAT 161..163
FT /note="5"
FT REPEAT 164..166
FT /note="6"
FT REPEAT 167..169
FT /note="7"
FT REPEAT 170..172
FT /note="8"
FT REPEAT 173..175
FT /note="9"
FT REPEAT 176..178
FT /note="10"
FT REGION 149..178
FT /note="10 X approximate repeats GMQ/P"
FT REGION 166..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 116
FT /note="A -> T (in Ref. 1; AAF03749)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="Q -> H (in Ref. 1; AAF03749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 25571 MW; 199285297F58BD51 CRC64;
MGTPETSREP CPDRILDDIG GAFGMGAVGG SAFHFIKGTY NSPKGSRFVG GTQSVSMNAP
RTGGSFAVWG GLFSTFDCTM VYLRQKEDPW NSIIAGAATG GFLSMRQGAG AASRSAIFGG
VLLALIEGAG IMLNKVLAQP QNMMMEDPGM QGMPGMQGMQ GMPGMPGMQG MPGMQGMQMG
QMQSQAQIRS ESQNQNTASS SSSSSWFGGL FDKKKEEVQP GSESKTEVLE SFDAPPVPSF
EFK
