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MGR1_KLULA
ID   MGR1_KLULA              Reviewed;         382 AA.
AC   Q6CUZ6; Q9URS9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Mitochondrial inner membrane i-AAA protease complex subunit MGR1;
GN   Name=MGR1; OrderedLocusNames=KLLA0C01089g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162.
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=10669871;
RX   DOI=10.1002/1097-0061(20000315)16:4<329::aid-yea533>3.0.co;2-2;
RA   Bao W.-G., Huo K.K., Li Y.Y., Fukuhara H.;
RT   "Protein disulfide isomerase genes of Kluyveromyces lactis.";
RL   Yeast 16:329-341(2000).
CC   -!- FUNCTION: Component of the mitochondrial inner membrane i-AAA protease
CC       complex required for mitochondrial inner membrane protein turnover.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the mitochondrial inner membrane i-AAA protease
CC       complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MGR1 family. {ECO:0000305}.
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DR   EMBL; CR382123; CAH01094.1; -; Genomic_DNA.
DR   EMBL; AJ243958; CAB51613.1; -; Genomic_DNA.
DR   RefSeq; XP_452243.1; XM_452243.1.
DR   AlphaFoldDB; Q6CUZ6; -.
DR   SMR; Q6CUZ6; -.
DR   STRING; 28985.XP_452243.1; -.
DR   PRIDE; Q6CUZ6; -.
DR   EnsemblFungi; CAH01094; CAH01094; KLLA0_C01089g.
DR   GeneID; 2892372; -.
DR   KEGG; kla:KLLA0_C01089g; -.
DR   eggNOG; ENOG502QR67; Eukaryota.
DR   HOGENOM; CLU_039216_0_0_1; -.
DR   InParanoid; Q6CUZ6; -.
DR   OMA; FYHEGID; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0031942; C:i-AAA complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
DR   InterPro; IPR013911; i-AAA_Mgr1.
DR   Pfam; PF08602; Mgr1; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..382
FT                   /note="Mitochondrial inner membrane i-AAA protease complex
FT                   subunit MGR1"
FT                   /id="PRO_0000324413"
FT   TOPO_DOM        1..44
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        45..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..129
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        130..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..382
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  44394 MW;  728EA57BE6A183DA CRC64;
     MAIYTSGTQS DNSEPVGNDP KFYTRPSLGL KLWGPLVPSS DNTTGLWSLV AIQTGLGLFL
     MQRFRKLGKK WVKRDIADFP SLNRFSTTHG DMYMTRHIPV QFGGTHSFNI RVGTRTGFWY
     SERFRTIRRV TYLLAGTLIL SQSMLEVSRL TLLKYDPWVE EAKSVREKQF FNDIVKYYHE
     GVDSTKFKAK DELSGQSISL NLPEVKQSIA VARAQAQAEN LVTKWFGPLD YKPQSFSEFL
     DKLEYYLNMT DFLNNLRRQK KNDKINSQLV KLEEENKRNR QRIHTLMAHA PARAIRTNQE
     VQDIYAIRKV LLHHDTESPN DIPLTEIWAI YNPWTNLALD TALSIKFFPS VIFNEDYYEH
     QKRLKDSEHV TSIENSEDER KP
 
 
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