MCD4_DEBHA
ID MCD4_DEBHA Reviewed; 990 AA.
AC Q6BWE3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=DEHA2B12012g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85480.2; -; Genomic_DNA.
DR RefSeq; XP_457476.2; XM_457476.1.
DR AlphaFoldDB; Q6BWE3; -.
DR SMR; Q6BWE3; -.
DR STRING; 4959.XP_457476.2; -.
DR EnsemblFungi; CAG85480; CAG85480; DEHA2B12012g.
DR GeneID; 2913427; -.
DR KEGG; dha:DEHA2B12012g; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q6BWE3; -.
DR OMA; TISHFCI; -.
DR OrthoDB; 270107at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000599; Chromosome B.
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:InterPro.
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..990
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246206"
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..479
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..541
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..594
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..681
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..747
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..811
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 833..854
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 905..921
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..990
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 952..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 137
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 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 990 AA; 112661 MW; 099F48214DA2B37E CRC64;
MNKNRQLLLF IGLAFHFFYL WSIFDIYFVS PLVHGMDNHK STDTPPAKRL FLIVGDGLRA
DKTFQKLKHP RTGETKYLAP YLRSLALNEG TWGISNTRMP TESRPGHVAM IAGFYEDVSA
VTKGWKENPV DFDSFFNQST HTYSFGSPDI LPMFAYGDNV VPGRIDTCMY GHEFEDFTQS
SIELDSFVFN HFNELMEDSA TNKTLHDELH QQGNVFFLHL LGPDTAGHAY RPYSAEYYDN
IEYIDEELSK LIPQIHEFFG DEESAFVFTA DHGMSDFGSH GDGHPDNTRT PLIAWGAGIN
KPKLLRDTPD AALLSTPQDP VASGYEANYF DTWKLDHLVR NDVNQADIAS LMAYLIGANY
PANSVGELPL DYINAESITK IKALYANSLA IVEQYLVKES EVYNHQFSFK PYDPFKQRSI
AEYKTQIETL ITLLEYGDLR EYDQKLKEAA AVDLSEELSK HALNGLNYLQ TYNWALLRSI
VTLGFFGWII YSFIIFLKLF ILTNRSILET KFSPALAGFF GFLAISINYV LYYQNSPFNY
YMYAAFPLYF WYTILNETAN LIEGLNQFLH GISVPTKLFV LVSFIGMYEG IVYGFFERFV
FSIIFVLIGL YPFFLRSRKI RFLQKLLWLS SCASMCVFTN LDPVKVESLT QINVGAAAAV
VASIFGARKV FERSIDNYNK TLVCLQIFVI LIMLYPTNVS VMSLQAREGL PAHSQIIGWV
TFVVSLFVLP VLYSLNPSAD YQLRLLSIFL TFVPTFIILT ISFELLFYVG YSLVLLQWLN
IEQSLKFSTR KIQKSRKLGL VPKGYWLQVI RITIIGFFFL QFAFFGTGNV ASISSFSLDS
VYRLIPIFDP FPMGALLMLK LIIPYILLST CLGIMNYRLE IRKFTISTLI ISTSDFLSLN
FFFLVRTEGS WLDIGVSISN YCLAILSSLF MLILELVSSI LLRGVELDSE ADEEADHDGA
SIDEANISEP EDIQSDAPIS ARVRRRTRKA
