(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 105.
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}.
DR   EMBL; AE016818; AAS52572.2; -; Genomic_DNA.
DR   RefSeq; NP_984748.2; NM_210102.2.
DR   STRING; 33169.AAS52572; -.
DR   PRIDE; Q757X5; -.
DR   EnsemblFungi; AAS52572; AAS52572; AGOS_AEL113C.
DR   GeneID; 4620935; -.
DR   KEGG; ago:AGOS_AEL113C; -.
DR   HOGENOM; HOG000170818; -.
DR   InParanoid; Q757X5; -.
DR   KO; K05285; -.
DR   OMA; GNQVVGW; -.
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;
DR   PRODOM; Q757X5.
DR   SWISS-2DPAGE; Q757X5.
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
//

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