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TIM9_CANAL
ID   TIM9_CANAL              Reviewed;          87 AA.
AC   Q59R24; A0A1D8PRE3; Q3MNZ4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM9;
GN   Name=TIM9; OrderedLocusNames=CAALFM_C703630CA;
GN   ORFNames=CaJ7.0415, CaO19.13988, CaO19.6696;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA   Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA   Mikami Y.;
RT   "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT   syntenic analysis against the Saccharomyces cerevisiae genome.";
RL   Genetics 170:1525-1537(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. Also required for the transfer of beta-
CC       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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC       TIM10, named soluble 70 kDa complex. Associates with the TIM22 complex,
CC       whose core is composed of TIM22 and TIM54. Interacts with the
CC       transmembrane regions of multi-pass transmembrane proteins in transit
CC       (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 TIM9 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; AP006852; BAE44866.1; -; Genomic_DNA.
DR   EMBL; CP017629; AOW30705.1; -; Genomic_DNA.
DR   RefSeq; XP_019331040.1; XM_019475495.1.
DR   AlphaFoldDB; Q59R24; -.
DR   SMR; Q59R24; -.
DR   STRING; 237561.Q59R24; -.
DR   GeneID; 3646243; -.
DR   KEGG; cal:CAALFM_C703630CA; -.
DR   CGD; CAL0000177007; TIM9.
DR   VEuPathDB; FungiDB:C7_03630C_A; -.
DR   eggNOG; KOG3479; Eukaryota.
DR   HOGENOM; CLU_141397_3_0_1; -.
DR   InParanoid; Q59R24; -.
DR   OMA; QDFLRMY; -.
DR   OrthoDB; 1627953at2759; -.
DR   Proteomes; UP000000559; Chromosome 7.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:EnsemblFungi.
DR   GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140318; F:protein transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:EnsemblFungi.
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   Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..87
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM9"
FT                   /id="PRO_0000228041"
FT   MOTIF           35..59
FT                   /note="Twin CX3C motif"
FT   DISULFID        35..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..55
FT                   /evidence="ECO:0000250"
FT   CONFLICT        78..87
FT                   /note="NALLMQQGPK -> KYVDLSRVTNGNMPLMIIIIYHQIILTNKLILL (in
FT                   Ref. 1; BAE44866)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   87 AA;  10202 MW;  5E78FE30BDA92055 CRC64;
     MDQLNVKEQQ EFQQIVEQKQ MKDFMNLYSN LVSRCFDDCV NDFTSNSLTS KETSCIAKCS
     EKFLKHSERV GQRFQEQNAL LMQQGPK
 
 
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