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TIM54_NEUCR
ID   TIM54_NEUCR             Reviewed;         468 AA.
AC   Q9C0Q7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim54;
DE   Flags: Precursor;
GN   Name=tim54; ORFNames=NCU07295;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=14668492; DOI=10.1091/mbc.e03-05-0272;
RA   Vasiljev A., Ahting U., Nargang F.E., Go N.E., Habib S.J., Kozany C.,
RA   Panneels V., Sinning I., Prokisch H., Neupert W., Nussberger S.,
RA   Rapaport D.;
RT   "Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are
RT   sufficient for translocation of the ADP/ATP carrier across membranes.";
RL   Mol. Biol. Cell 15:1445-1458(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Essential component of the TIM22 complex, a complex that
CC       mediates the import and insertion of multi-pass transmembrane proteins
CC       into the mitochondrial inner membrane. The TIM22 complex forms a twin-
CC       pore translocase that uses the membrane potential as external driving
CC       force (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of
CC       tim22 and tim54, associated with the 70 kDa heterohexamer composed of
CC       tim9 and tim10 (or tim8 and tim13). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TIM54 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK26641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAK26642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF343072; AAK26641.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF343073; AAK26642.1; ALT_INIT; mRNA.
DR   EMBL; CM002239; EAA32913.2; -; Genomic_DNA.
DR   RefSeq; XP_962149.2; XM_957056.3.
DR   AlphaFoldDB; Q9C0Q7; -.
DR   SMR; Q9C0Q7; -.
DR   STRING; 5141.EFNCRP00000007146; -.
DR   EnsemblFungi; EAA32913; EAA32913; NCU07295.
DR   GeneID; 3878298; -.
DR   KEGG; ncr:NCU07295; -.
DR   VEuPathDB; FungiDB:NCU07295; -.
DR   HOGENOM; CLU_039097_1_0_1; -.
DR   InParanoid; Q9C0Q7; -.
DR   OMA; EEKEWHK; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IBA:GO_Central.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR   InterPro; IPR021056; Mt_import_IM_translocase_Tim54.
DR   Pfam; PF11711; Tim54; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW   Reference proteome; Transit peptide; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..52
FT                   /note="Mitochondrion"
FT   CHAIN           53..468
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim54"
FT                   /id="PRO_0000228017"
FT   TOPO_DOM        53..58
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..468
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  53075 MW;  D21ADC2AAFDE3434 CRC64;
     MADPVPPAST APPAAPAATT ATPPPPPPPP PPKALRPQNQ ALRMLGLPNL PNKLPSRNWM
     IFWTVSASIT AAIIYDRREK RRNIAKWRHA VEHLAAEPIT DKLGLEQPRK LTIYLSAPPG
     DGLRVAQDHY TEYVKPVLAA SGLDWEFVQG RREGDVRAVV AERLRKVRRG WENKEEQDPN
     REPTKDELIE IYRQQRGIKD YEGVRGDVVI GRHTWKEYLR GLHEGWLGPL VAPAEPAPLP
     PTPAPAAAEG STSTEDKPAE EKKEEEAPKP KRPPQPKPYN TTSDYSSETL HPLTPQELTP
     AVPIREPHIL GFLNTPTRMV RFFNRRSLAD DIGREVAAVC LATHREFQQQ TNPDAPSTDS
     VQYEQAKELE WEEQDWPKKV WKEDEADADK EVTEKIHIKP VVMDPRLAHR MRRFALTPED
     EDRVSKIKVP EEEVEGWIKG SLRKACHWGY DKAFNKKKLV PLEDKDVE
 
 
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