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INA17_CANGA
ID   INA17_CANGA             Reviewed;         164 AA.
AC   Q6FRU5;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Inner membrane assembly complex subunit 17 {ECO:0000250|UniProtKB:Q02888};
DE   Flags: Precursor;
GN   Name=INA17 {ECO:0000250|UniProtKB:Q02888}; OrderedLocusNames=CAGL0H05819g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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).
CC   -!- FUNCTION: Component of the INA complex (INAC) that promotes the
CC       biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the
CC       assembly of the peripheral stalk and promotes the assembly of the
CC       catalytic F(1)-domain with the membrane-embedded F(0)-domain.
CC       {ECO:0000250|UniProtKB:Q02888}.
CC   -!- SUBUNIT: Component of the inner membrane assembly (INA) complex,
CC       composed of INA17 and INA22. Interacts with a subset of F(1)F(0)-ATP
CC       synthase subunits of the F(1)-domain and the peripheral stalk.
CC       {ECO:0000250|UniProtKB:Q02888}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q02888}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the INA17 family. {ECO:0000305}.
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DR   EMBL; CR380954; CAG59982.1; -; Genomic_DNA.
DR   RefSeq; XP_447049.1; XM_447049.1.
DR   AlphaFoldDB; Q6FRU5; -.
DR   STRING; 5478.XP_447049.1; -.
DR   EnsemblFungi; CAG59982; CAG59982; CAGL0H05819g.
DR   GeneID; 2888642; -.
DR   KEGG; cgr:CAGL0H05819g; -.
DR   CGD; CAL0131788; CAGL0H05819g.
DR   VEuPathDB; FungiDB:CAGL0H05819g; -.
DR   eggNOG; ENOG502S3U1; Eukaryota.
DR   HOGENOM; CLU_127263_1_0_1; -.
DR   InParanoid; Q6FRU5; -.
DR   OMA; HYVWWKL; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:1990524; C:INA complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990677; C:mitochondrial inner membrane assembly complex; IEA:EnsemblFungi.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IEA:EnsemblFungi.
PE   3: Inferred from homology;
KW   Chaperone; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..164
FT                   /note="Inner membrane assembly complex subunit 17"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000399878"
FT   TOPO_DOM        29..97
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q02888"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..164
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q02888"
FT   COILED          121..149
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   164 AA;  19359 MW;  F60CE52B7C4ADE85 CRC64;
     MIKTAKISTL RLAITRNARN LSFTTLVRSP EVDNSKIKTL EDLTRLETLE GVDPELIKRL
     INEKTQEFNT QDELKLLKSM QMEQDRLNEV PLKRFTRPLW IFILMASTFY LGAHLVWWKL
     AYEKKEVELK HKVDSLETTL KDVMKEKATG PTPCNNKKSW YKFW
 
 
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