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TIM13_ASPFU
ID   TIM13_ASPFU             Reviewed;         113 AA.
AC   Q4X0V2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim13;
GN   Name=tim13; ORFNames=AFUA_2G12190;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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 is non essential and only mediates the import of few
CC       proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial
CC       and mediates the import of much more proteins (By similarity).
CC       {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 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 TIM13 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; AAHF01000001; EAL93513.1; -; Genomic_DNA.
DR   RefSeq; XP_755551.1; XM_750458.1.
DR   AlphaFoldDB; Q4X0V2; -.
DR   SMR; Q4X0V2; -.
DR   STRING; 746128.CADAFUBP00002727; -.
DR   EnsemblFungi; EAL93513; EAL93513; AFUA_2G12190.
DR   GeneID; 3513485; -.
DR   KEGG; afm:AFUA_2G12190; -.
DR   VEuPathDB; FungiDB:Afu2g12190; -.
DR   eggNOG; KOG1733; Eukaryota.
DR   HOGENOM; CLU_141397_0_1_1; -.
DR   InParanoid; Q4X0V2; -.
DR   OMA; RCISQCM; -.
DR   OrthoDB; 1566384at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140318; F:protein transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
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..113
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim13"
FT                   /id="PRO_0000228070"
FT   MOTIF           47..70
FT                   /note="Twin CX3C motif"
FT   DISULFID        47..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  12089 MW;  A88257F585C86AC4 CRC64;
     MAIWGSSSSN TASSGEADIK THLMNQVRQE AAVTNARNLI GKVNEHCFEA CIPNPGTSLS
     SAEHTCLSQC MEKYISFWNA VSRGYIARLA NERKAYGGGA LDASFVQSGE SSL
 
 
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