MCD4_ASHGO
ID MCD4_ASHGO Reviewed; 925 AA.
AC Q757X5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=AEL113C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 360.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52572.2; -; Genomic_DNA.
DR RefSeq; NP_984748.2; NM_210102.2.
DR AlphaFoldDB; Q757X5; -.
DR SMR; Q757X5; -.
DR STRING; 33169.AAS52572; -.
DR EnsemblFungi; AAS52572; AAS52572; AGOS_AEL113C.
DR GeneID; 4620935; -.
DR KEGG; ago:AGOS_AEL113C; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q757X5; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; 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; 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..925
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246200"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..516
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..574
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..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..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..687
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..775
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 797..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..848
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 870..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 907..925
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 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 925 AA; 105647 MW; 10D4D8F6FA727E5C CRC64;
MWNKHRLAFI LVGLLFHLFY LRSIFDIYFV SPLVHGMRQF KSNEEPPAKR LFLIVGDGLR
ADTSFDKVKH PVTGKTEFLA PYLRSLVEHN ATYGISHTRM PTESRPGHVA MIAGFYEDVS
AVTKGWKENP VDFDSVFNQS THTYSFGSPD ILPMFKSGAS DPTKVDAWMY GHEFEDFTQS
SIELDAYVFR HMDALFRNAT VDSKLRHEMM QDGNVFFLHL LGCDTAGHSY RPYSAEYYDN
VKYIDSQLER LVPKVREFFG DDDTAFVFTA DHGMSAFGSH GDGHPNNTRT PLVAWGAGLN
RPVLNDVPVY DNYTENWDLA HVRRNDVNQA DIASLMSYLI GLNYPTNSVG ELPLAYVNGT
ERTKLNALYK NALSILEQYL VKETEMIQSQ LVYKEYPKFA QKSHSSYIQE IEHLIDRIAN
GEEDLEPEAI ALSEELMKTA LEGLQYLTTY NWRFIRSIVT LGFIGWITYS FTIFLRLFIL
EKQYAMKTSP QNLASFGALT AALNYVLYYQ RSPFNYYMYL LFPLFFWSQI LTNSTILHDG
IREMFKGVSM LQRIGICALI VSIYEGIVYG YFDRWIFTII FNLLALYPFF CGIKDAKTNM
FWGANSMALS IFTLFDAVKI ESLTQINVSG LLLVASGLYA LWRVSKKINS HTKIVILLQI
LLLAMMLAVT NKSVTSLQQR AGLPTDAKIA GWVILTLSLS LMPLLHYLKP SNDYQVRVLV
IYLTFAPTFL ILTISFESFF YLLFTNYLML WIEIESKIKA QNIAKNSQNW LQLLRISIIG
FFLLQFAFFG TGNVASISSF SLDSVYRLMP VFDPFPMGAL LILKIMIPYI LLSTALGIMN
LKLNIKDYTV SSLILSTSDV LSLNFFYLLR TEGSWLDIGV TISNYCLAIL SSLFMIVLEL
FSHFLLKNVR DNGMDIAASK QQKRH
