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Database: UniProt/TrEMBL
Entry: Q6FXM9_CANGA
LinkDB: Q6FXM9_CANGA
Original site: Q6FXM9_CANGA 
ID   Q6FXM9_CANGA            Unreviewed;       134 AA.
AC   Q6FXM9;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   09-JUL-2014, entry version 49.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2;
DE            Short=Oligosaccharyl transferase subunit OST2;
DE            EC=2.4.99.18;
GN   OrderedLocusNames=CAGL0B04499g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   mitosporic Nakaseomyces.
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;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Essential subunit of the N-oligosaccharyl transferase
CC       (OST) complex which catalyzes the transfer of a high mannose
CC       oligosaccharide from a lipid-linked oligosaccharide donor to an
CC       asparagine residue within an Asn-X-Ser/Thr consensus motif in
CC       nascent polypeptide chains (By similarity).
CC   -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
CC       L-asparagine = dolichyl diphosphate + a glycoprotein with the
CC       oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC       protein L-asparagine.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family.
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DR   EMBL; CR380948; CAG58066.1; -; Genomic_DNA.
DR   RefSeq; XP_445166.1; XM_445166.1.
DR   GeneID; 2886658; -.
DR   KEGG; cgr:CAGL0B04499g; -.
DR   HOGENOM; HOG000211854; -.
DR   KO; K12668; -.
DR   OMA; FIICVGQ; -.
DR   OrthoDB; EOG757D9B; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR   GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; PTHR10705; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Endoplasmic reticulum; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   134 AA;  14862 MW;  C05508934312EA21 CRC64;
     MAGPKKVSSS KSSKDAQSGE VFNDFKEAIN SSMKAYTTQV EGNNKLKLID IFCVFLVLVG
     GIQFLFALLV RDSFPFNAFL AGFIMCVGQF VLLISLRLQI LNQIEFPGIS SNRAFAEFII
     ASLTLHFICL HFIN
//
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