MCD4_YARLI
ID MCD4_YARLI Reviewed; 932 AA.
AC Q6C0Z3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=YALI0F20570g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG78478.1; -; Genomic_DNA.
DR RefSeq; XP_505669.1; XM_505669.1.
DR AlphaFoldDB; Q6C0Z3; -.
DR STRING; 4952.CAG78478; -.
DR EnsemblFungi; CAG78478; CAG78478; YALI0_F20570g.
DR GeneID; 2908691; -.
DR KEGG; yli:YALI0F20570g; -.
DR VEuPathDB; FungiDB:YALI0_F20570g; -.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q6C0Z3; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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..932
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246211"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..456
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..509
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..577
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..627
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..696
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..786
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..859
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 881..900
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 922..932
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 932 AA; 104114 MW; C7643F30CDEE0C43 CRC64;
MISLNKKLVL LVGVIFHVAF MWSIFDIYFV SPLIHGMKHH QSTATPPAKR LFLIVGDGLR
ADKAFEKVRH PTTGESEYLA PFLRSKVMSD ATFGISHTRM PTESRPGHVA LIAGFYEDVS
AVTKGWKENP VDFDSVFNQS RHTYSLGSPD ILPMFKHGAE DQSRIDAIMY GHDFEDFTKG
SIELDAFVFD HLDEIFDKSK TNKTLDDQLR SDKTVFFLHL LGIDTAGHSY RPYSAEYYDN
IKYIDENIEK LVDKVNKFYN DDEQTAWVFT ADHGMSDWGS HGDGHPDNTR TPLIAWGAGV
NKPIPAFEDK GNHDDYSEVW DLPVKRNDVN QADIASLMSY LVGLNYPSNS VGELPLAFVN
ATSETKALAI RNNALALVEQ YLVKEEQQKG SQIIFKPYPP LSDAGKTIDE RLAHIDELIA
QGLDQESIVA SEELMTYAIT GLKYLQTYNW LFLRTLVTIG FFGWIAVAFC SYLLAFVVQS
DKPFTTSLPL KGVAYVALAI LSGFFVFQKS PLHYHLYAVF PVVFWEAVLQ RRTAVAEGIS
ILARRSTSKA PALAAILDIG LSLVLLEAIV YGYFHREIFS VCFGLATLWP FVHNFTVAKR
EWPTTLAWVV MCAIMSSFTL LEVVKVESIE QILLSGALML VIGLVFTIHL QRKLALAAST
VCVLFAQILL VVATMYFTRE SVESLTARNG LPLFSQVGGW ISLLLSLAVP FLHFLGSDAK
DYRLRLLIIF LAFGPTFVIL TISWEGFFYV CFFAILVIWI ELETQMRDAR VTPQTRADLT
PGDFRMALFT FFMSQIGFFG IGNIASISSF SLDSVYRLIP VFDPFSMGAL LMFKILVPFA
VLSACLGILN LKLGVPPSAL FSMVLCVSDI LTLNFFYLVV DEGSWLDIGT GISHYCIASG
LSLFMMVLEY LSGVLVAGVT IAPHVSKIKK DM
