TIM8_DROME
ID TIM8_DROME Reviewed; 88 AA.
AC Q9Y1A3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8;
GN Name=Tim8; ORFNames=CG1728;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SD;
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=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
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; AF142424; AAD39162.1; -; mRNA.
DR EMBL; AE014298; AAF48036.1; -; Genomic_DNA.
DR EMBL; AY118649; AAM50018.1; -; mRNA.
DR RefSeq; NP_001285120.1; NM_001298191.1.
DR RefSeq; NP_572713.1; NM_132485.4.
DR AlphaFoldDB; Q9Y1A3; -.
DR SMR; Q9Y1A3; -.
DR BioGRID; 58493; 14.
DR DIP; DIP-20805N; -.
DR IntAct; Q9Y1A3; 2.
DR STRING; 7227.FBpp0073338; -.
DR PaxDb; Q9Y1A3; -.
DR PRIDE; Q9Y1A3; -.
DR DNASU; 32081; -.
DR EnsemblMetazoa; FBtr0073482; FBpp0073338; FBgn0027359.
DR EnsemblMetazoa; FBtr0343640; FBpp0310233; FBgn0027359.
DR GeneID; 32081; -.
DR KEGG; dme:Dmel_CG1728; -.
DR UCSC; CG1728-RA; d. melanogaster.
DR CTD; 32081; -.
DR FlyBase; FBgn0027359; Tim8.
DR VEuPathDB; VectorBase:FBgn0027359; -.
DR eggNOG; KOG3489; Eukaryota.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q9Y1A3; -.
DR OMA; SKQKVQM; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q9Y1A3; -.
DR BioGRID-ORCS; 32081; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tim8; fly.
DR GenomeRNAi; 32081; -.
DR PRO; PR:Q9Y1A3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027359; Expressed in egg chamber and 17 other tissues.
DR ExpressionAtlas; Q9Y1A3; baseline and differential.
DR Genevisible; Q9Y1A3; DM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; ISS:FlyBase.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:FlyBase.
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 3: Inferred from homology;
KW Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..88
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8"
FT /id="PRO_0000193590"
FT MOTIF 38..61
FT /note="Twin CX3C motif"
FT DISULFID 38..61
FT /evidence="ECO:0000250"
FT DISULFID 42..57
FT /evidence="ECO:0000250"
SQ SEQUENCE 88 AA; 10062 MW; 7FA4CEABDA7CDF0A CRC64;
MSDFENLSGN DKELQEFLLI EKQKAQVNAQ IHEFNEICWE KCIGKPSTKL DHATETCLSN
CVDRFIDTSL LITQRFAQML QKRGGGDL
