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T10B_DROME
ID   T10B_DROME              Reviewed;         117 AA.
AC   Q9Y0V3; A4V4S9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10B;
DE   AltName: Full=Mitochondrial import inner membrane translocase subunit Tim9B;
DE   AltName: Full=Tim10b;
GN   Name=Tim9b; Synonyms=tim9; ORFNames=CG17767;
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].
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).
CC   -!- FUNCTION: Component of the TIM22 complex, a complex that mediates the
CC       import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. The TIM22 complex forms a twin-pore
CC       translocase that uses the membrane potential as the external driving
CC       force. In the TIM22 complex, it may act as a docking point for the
CC       soluble 70 kDa complex that guides the target proteins in transit
CC       through the aqueous mitochondrial intermembrane space (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of
CC       Tim22, associated with peripheral protein Tim9b/Tim10b and the 70 kDa
CC       heterohexamer. In most cases, the 70 kDa complex is composed of TIMM9
CC       and TIMM10 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {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 Tim9b/Tim10b from the cytoplasm into the
CC       mitochondrion, the Cys residues probably coordinate zinc, thereby
CC       preventing folding and allowing its transfer across the mitochondrial
CC       outer membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR   EMBL; AF150104; AAD40010.1; -; mRNA.
DR   EMBL; AE014298; AAF48984.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAO41712.1; -; Genomic_DNA.
DR   RefSeq; NP_001027074.1; NM_001031903.2.
DR   RefSeq; NP_001027075.1; NM_001031904.3.
DR   AlphaFoldDB; Q9Y0V3; -.
DR   SMR; Q9Y0V3; -.
DR   STRING; 7227.FBpp0074536; -.
DR   PaxDb; Q9Y0V3; -.
DR   DNASU; 3772213; -.
DR   EnsemblMetazoa; FBtr0074767; FBpp0074536; FBgn0027358.
DR   EnsemblMetazoa; FBtr0344072; FBpp0310503; FBgn0027358.
DR   GeneID; 3772213; -.
DR   KEGG; dme:Dmel_CG17767; -.
DR   UCSC; CG17767-RB; d. melanogaster.
DR   CTD; 3772213; -.
DR   FlyBase; FBgn0027358; Tim9b.
DR   VEuPathDB; VectorBase:FBgn0027358; -.
DR   eggNOG; KOG3479; Eukaryota.
DR   GeneTree; ENSGT00450000040326; -.
DR   HOGENOM; CLU_141397_2_1_1; -.
DR   InParanoid; Q9Y0V3; -.
DR   OMA; CFNRCVD; -.
DR   PhylomeDB; Q9Y0V3; -.
DR   Reactome; R-DME-1268020; Mitochondrial protein import.
DR   BioGRID-ORCS; 3772213; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; Tim9b; fly.
DR   GenomeRNAi; 3772213; -.
DR   PRO; PR:Q9Y0V3; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027358; Expressed in testis and 11 other tissues.
DR   Genevisible; Q9Y0V3; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140318; F:protein transporter activity; ISS:FlyBase.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:FlyBase.
DR   GO; GO:0071456; P:cellular response to hypoxia; IMP: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   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; SSF144122; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..117
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim10B"
FT                   /id="PRO_0000193604"
FT   REGION          75..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           22..46
FT                   /note="Twin CX3C motif"
FT   COMPBIAS        75..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   117 AA;  13520 MW;  3327A332075A57E5 CRC64;
     MDSNLRNLKD FFTLYNKVTE LCFSRCVDNL SQRDLGGHED LCVDRCVTKF ARFNQNMMKV
     YVDVQTTINA KRMEEMEENA RKAEQQQREQ EKERLKEAAA TAVLTPVQPP VAGNLSM
 
 
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