MCD4_CANGA
ID MCD4_CANGA Reviewed; 921 AA.
AC Q6FJ81;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=CAGL0M08448g;
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 first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor (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. PIGN subfamily.
CC {ECO:0000305}.
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DR EMBL; CR380959; CAG62689.1; -; Genomic_DNA.
DR RefSeq; XP_449713.1; XM_449713.1.
DR AlphaFoldDB; Q6FJ81; -.
DR SMR; Q6FJ81; -.
DR STRING; 5478.XP_449713.1; -.
DR EnsemblFungi; CAG62689; CAG62689; CAGL0M08448g.
DR GeneID; 2891272; -.
DR KEGG; cgr:CAGL0M08448g; -.
DR CGD; CAL0136323; CAGL0M08448g.
DR VEuPathDB; FungiDB:CAGL0M08448g; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q6FJ81; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
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:0015867; P:ATP transport; IEA:EnsemblFungi.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..921
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246204"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..516
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..575
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..684
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..777
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 799..819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..849
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..878
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 879..899
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 900..921
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 921 AA; 104729 MW; C4C6C79B953798FE CRC64;
MKNNTRFTLI VVGVLFHLLY LWSIFDIYFI SPLVHGMEQK ISTNNPPAKR LFLIVGDGLR
ADTTFDKITH PVTKKADYLA PFIRSLVQNN ATYGISHTRM PTESRPGHVA MIAGFYEDVS
AVTKGWKENP VDFDSFFNQT AHTYSFGSPD ILPMFKDGAS DPNKVDAWMY GHEYEDFTQS
SIELDAYVFR HLDQLFKNSS TDKELDKQIR QDGNAFFLHL LGCDTAGHSY RPYSAEYYDN
VIYIDKQVEK LVKQVEEFFG DNDTAFIFTA DHGMSAFGSH GDGHPNNTRT PLVAWGAGLN
RPVRLDTPEF DEYTENWNLA NIKRNDVKQA DIAALMSYLI GTNYPANSVG ELPLAYIEGS
EGQKLEALLN NAESILEQYR VKENEVINSQ FVYKIYPKFA EKSPTEYLKE IKELIKKIEN
GEESLEPEAI RLTEELMKVT LEGLHYLTTY NWRFIRTIVT FGFLGWICYS FMIFLKLFIL
NNSQTTHPSI LNISIFTSLG LILNYILFYQ KSPLNFYLYL IFPLFFWSKI FSNTAIIRDG
VNEFFKGISK AESVIIGLTI ISIYEGIVYG FFHRWILSLI LVSFAFYPLV CGVTDLFTNL
LWILTSVGLS SFTLLDAVKI ENLQQIQVAG ILIVLSSAYA VMRLSQDISK YTQHLLSIQI
FLVSGMLHFT SKSVISLQKR EGLPAFAQVG GWAILVISLT IMPFLHYLKP NNNYQVRLLT
IYLTFAPSFI ILSISFEALF YFIFTAYIVQ WLQIEKNIKV LKDEQKSDSN GIQLLRVAII
GFFLQQIAFF GTGNVASISS FSLDSVYRLL PVFDPFPMGA LLMLKLIIPY VLLSCGLGIM
NIQLDIKDYT ISSLIISTSD ILSLNFFYLL KTEGSWLDIG VTISNYCLAI LSSLFMLILE
IVGHQLLKNV TRATSSQKKT N
