TIM8_ARATH
ID TIM8_ARATH Reviewed; 77 AA.
AC Q9XGY4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM8;
GN Name=TIM8; OrderedLocusNames=At5g50810; ORFNames=K7B16.3;
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].
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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 TIM8-
CC TIM13 complex mediates the import of some proteins while the
CC predominant TIM9-TIM10 70 kDa complex mediates the import of much more
CC proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM8 and 3 copies of
CC TIM13, named soluble 70 kDa complex. Associates with the TIM22 complex,
CC whose core is composed of TIM22 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:14730085}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, young cotyledons and
CC leaves. {ECO:0000269|PubMed:14730085}.
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 TIM8 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; AF150083; AAD39990.1; -; mRNA.
DR EMBL; AB025617; BAB08904.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95995.1; -; Genomic_DNA.
DR EMBL; BT002881; AAO22698.1; -; mRNA.
DR EMBL; BT004405; AAO42399.1; -; mRNA.
DR EMBL; AY087301; AAM64853.1; -; mRNA.
DR RefSeq; NP_199894.1; NM_124459.4.
DR AlphaFoldDB; Q9XGY4; -.
DR SMR; Q9XGY4; -.
DR BioGRID; 20399; 3.
DR IntAct; Q9XGY4; 1.
DR STRING; 3702.AT5G50810.1; -.
DR iPTMnet; Q9XGY4; -.
DR MetOSite; Q9XGY4; -.
DR PaxDb; Q9XGY4; -.
DR PRIDE; Q9XGY4; -.
DR ProteomicsDB; 234375; -.
DR DNASU; 835153; -.
DR EnsemblPlants; AT5G50810.1; AT5G50810.1; AT5G50810.
DR GeneID; 835153; -.
DR Gramene; AT5G50810.1; AT5G50810.1; AT5G50810.
DR KEGG; ath:AT5G50810; -.
DR Araport; AT5G50810; -.
DR TAIR; locus:2157931; AT5G50810.
DR eggNOG; KOG3489; Eukaryota.
DR HOGENOM; CLU_141397_1_1_1; -.
DR InParanoid; Q9XGY4; -.
DR OMA; SKQKVQM; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q9XGY4; -.
DR PRO; PR:Q9XGY4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGY4; baseline and differential.
DR Genevisible; Q9XGY4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005758; C:mitochondrial intermembrane space; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 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; Disulfide bond; Metal-binding; Mitochondrion;
KW Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..77
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM8"
FT /id="PRO_0000193591"
FT MOTIF 35..59
FT /note="Twin CX3C motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 35..59
FT /evidence="ECO:0000250"
FT DISULFID 39..55
FT /evidence="ECO:0000250"
SQ SEQUENCE 77 AA; 8750 MW; 47E5B41ED90D0EFF CRC64;
MDPSMANNPE LLQFLAQEKE RAMVNEMVSK MTSVCWDKCI TSAPGSKFSS SESSCLTHCA
QRYMDMSMII MKRFNSQ
