MCD4_KLULA
ID MCD4_KLULA Reviewed; 919 AA.
AC Q6CW36;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=KLLA0B07249g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH02246.1; -; Genomic_DNA.
DR RefSeq; XP_451853.1; XM_451853.1.
DR AlphaFoldDB; Q6CW36; -.
DR SMR; Q6CW36; -.
DR STRING; 28985.XP_451853.1; -.
DR EnsemblFungi; CAH02246; CAH02246; KLLA0_B07249g.
DR GeneID; 2897133; -.
DR KEGG; kla:KLLA0_B07249g; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q6CW36; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000598; Chromosome B.
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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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; IPR037671; PIGN_N.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF04987; PigN; 1.
DR Pfam; PF00884; Sulfatase; 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..919
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246209"
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..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..510
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..598
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..653
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..718
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..815
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 837..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..882
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 919 AA; 105516 MW; 273E77AE37988BEE CRC64;
MWSRHRLYFI VAGVLFHLFY LWSIFDIYFV SPLVHGMKQH QSTDEAPAKR LFLIVGDGLR
ADTTFDKILH PVTGEHDYLA PYIRDLVRNE ATYGVSHTRM PTESRPGHVA MIAGFYEDVS
AVTKGWQENP VDFDSFFNQS KHTYSFGSPD ILPMFKDGAT PNKVDAWMYG HEFEDFTQSS
IELDAFVFRH IYELFNNTKS NKTLETEIKQ DGNVFFLHLL GCDTAGHSYR PYSAEYYDNV
KYIDKEVKLL VEKVHEFFDD EDTAFIFTAD HGMSAFGSHG DGHPNNTRTP LVAWGAGINK
PVKNQAPIFD NYTENWNLAD IKRNDVNQAD IASLMSYLIG ANYPVNSVGE LPLNFIDAPE
DKKLNALFNN AKAILEQYLV KEQEIIASQF VYKEYEAFVE IPYQEYLQQI ESLIERIAKG
ENELEPDAIK LTEELMKVTL DGLAYLTTYN WRFIRTIVTL GFLGWIVYSF SIFLRLFILN
RDYNSHKSLL NYFIFGSLTI ILNYVLYYQK APFNYYMYLF FPLIFWSEIF TDRVVLDDGV
KEFLKGISIP KRIILVSAII LVYESIVYAF FDRWIFSLIF NMLSFYPLIC GYRDWKRNTL
WFITGAAISV FTLLDAVKIE SLTQINIASG LIVLTALSGF LHLRKQLNSY TTTVFICQIL
LVILMVLATN KSIVSLQNRT GLPRDAQVAG WVILVVSLLL MPLIHYMKPN NNYKVRMLII
FLTFAPTFII LTISFESFFY LVFSAYIVQW IEIESKLKEQ TPNTSHYKQL IRVTIIGFFL
LQNAFFGTGN VASISSFSLD SVYRLMPIFD PFPMGALLVI KLIIPYIILS AGLGILNLKL
HIKDYTISTL IISTSDILSL NFFYLLKTEG SWLDIGITIS NYCLAILSSL FMLILEIVAH
VVLKNVQLSK PVIASKKTN
