位置:首页 > 蛋白库 > GPI11_CANGA
GPI11_CANGA
ID   GPI11_CANGA             Reviewed;         217 AA.
AC   Q6FSD1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glycosylphosphatidylinositol anchor biosynthesis protein 11;
GN   Name=GPI11; OrderedLocusNames=CAGL0H01485g;
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: Acts in the GPI biosynthetic pathway between GlcNAc-PI
CC       synthesis and GPI transfer to protein. {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380954; CAG59796.1; -; Genomic_DNA.
DR   RefSeq; XP_446863.1; XM_446863.1.
DR   AlphaFoldDB; Q6FSD1; -.
DR   STRING; 5478.XP_446863.1; -.
DR   EnsemblFungi; CAG59796; CAG59796; CAGL0H01485g.
DR   GeneID; 2888443; -.
DR   KEGG; cgr:CAGL0H01485g; -.
DR   CGD; CAL0131732; CAGL0H01485g.
DR   VEuPathDB; FungiDB:CAGL0H01485g; -.
DR   eggNOG; KOG3144; Eukaryota.
DR   HOGENOM; CLU_111662_0_0_1; -.
DR   InParanoid; Q6FSD1; -.
DR   OMA; FNCDFKV; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009580; GPI_biosynthesis_protein_Pig-F.
DR   Pfam; PF06699; PIG-F; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..217
FT                   /note="Glycosylphosphatidylinositol anchor biosynthesis
FT                   protein 11"
FT                   /id="PRO_0000191764"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   217 AA;  25041 MW;  7F9B7FC1C6D9060A CRC64;
     MPVKKRTPLK HKSVSFSDDI TQTQHNHHHR KKQNGERPPV FIRKTWLTIP WHLIALVYIY
     VKVFNNYNTA ELLACLVPLQ ILYTIFQFNK ATIYGNKRLK FNYSLAAISI LACIVLSIPV
     VVIIILFGAP LLELLWETWL LALHCSFLAY PAVYSVLNCD FKVGLWKRYF ILIVVGCWIS
     CVVIPLDWDR DWQAWPIPIV IGAYLGAFVG FAYGAYL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024