GPI7_CANGA
ID GPI7_CANGA Reviewed; 842 AA.
AC Q6FPB2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN Name=LAS21; Synonyms=GPI7; OrderedLocusNames=CAGL0J05236g;
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: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose (By similarity).
CC {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 PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; CR380956; CAG60883.1; -; Genomic_DNA.
DR RefSeq; XP_447932.1; XM_447932.1.
DR AlphaFoldDB; Q6FPB2; -.
DR SMR; Q6FPB2; -.
DR STRING; 5478.XP_447932.1; -.
DR PRIDE; Q6FPB2; -.
DR EnsemblFungi; CAG60883; CAG60883; CAGL0J05236g.
DR GeneID; 2889505; -.
DR KEGG; cgr:CAGL0J05236g; -.
DR CGD; CAL0132810; LAS21.
DR VEuPathDB; FungiDB:CAGL0J05236g; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q6FPB2; -.
DR OMA; HIGHKTG; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IEA:EnsemblFungi.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037674; PIG-G_N.
DR InterPro; IPR039527; PIGG/GPI7.
DR InterPro; IPR045687; PIGG/GPI7_C.
DR PANTHER; PTHR23072; PTHR23072; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..842
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246194"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 842 AA; 95770 MW; 7072063051B0DFC2 CRC64;
MLFLLVVAHA IAVLIFGCGF FPQKKVLDGH AALDGTHARD PVFDKLVVVV VDAMRSDFLF
DASISKFHFI HEKLADGSAW GFTAHSNPPT VTLPRLKGIT TGSTPNFLDA ILNVAEDDTS
SSLLAQDSWL WQFRNNAGKR IRFFGDDTWL KLFPPVEANE DSQTMFDEYE GTNSFFVSDF
TQVDLNVTRH IDRQLRETSE WDVLILHYLG LDHIGHKDGP YSRFMGPKHE EMDSIIRKLY
DELDMQSTLL VLMGDHGMND LGNHGGSSAG ETSAGMVFLS DKLAAYKPSK EQSSAKEFPM
KIPSLNAGEE KTFHYLKKIQ QIDVVPTISS LFNVAIPKNN VGVIIPEFLQ LFKDVSLQKA
IVKENWNQLS GLTKGKTQIM EETKNFVIED VIKNMKDVQE NLAKTATDYN YPLLFIGCFL
SIVITGTIYY RYARHVAINI NTSILIAIAA LMGISVFGSS FIEEEHQFWW WIITGLVLLS
MVNLNFSSWK SHIIVLFCLR LIRGWNNSGQ KYTYDNVIAN LLKGNIDALW WLNLITVTVV
GLNLKSLRFG NHTVSLLGFS DLLSMGLLSM ITFLYKVNWS IVNGERVPDL FYKWVLETAS
LIVEDATLYR EEDLIHTALI PLARIFFKLF FAVLVSRLMI QKFFQVSDIS KSLAVVSRYV
TIFLVFQTPS HNIGLFLFFE IINEITVHII RERYQSDYLL AVIFGIILQF FTFFQSGGTN
SIATVDLSNA YNGVSENYNI YVVGLMMCIS NFAPTIYWSF YNWRITYANA NSSRWQTLVA
AKYPFIIIQS TIGCCLLLAC IILRYHLFIW SVFSPKLCYY MVWTIFVGII VHWIPEILLL
LT
