MCD4_GIBZE
ID MCD4_GIBZE Reviewed; 981 AA.
AC Q4ILH3; A0A098D853; A0A0E0RSB6; V6R072;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; ORFNames=FGRRES_01935, FGSG_01935;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231663; ESU07302.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF74141.1; -; Genomic_DNA.
DR RefSeq; XP_011317787.1; XM_011319485.1.
DR AlphaFoldDB; Q4ILH3; -.
DR SMR; Q4ILH3; -.
DR STRING; 5518.FGSG_01935P0; -.
DR EnsemblFungi; ESU07302; ESU07302; FGSG_01935.
DR GeneID; 23549346; -.
DR KEGG; fgr:FGSG_01935; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G04669; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q4ILH3; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000070720; Chromosome 1.
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:0008484; F:sulfuric ester hydrolase 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; 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..981
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246208"
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..464
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..587
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..638
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..708
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..819
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..892
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..981
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 981 AA; 108331 MW; C7BEED3850C45ED5 CRC64;
MAGSSRIGFM AIAVAFHLVY ILSIFDIYFV SPIVTGMKLF GVERPHESPK APADRLVLFV
GDGLRADKAF QAHPEPYPES DQDLVPRHLA PYLRSRVLEH GTFGVSHTRV PTESRPGHVA
LIAGLYEDVS AVATGWKMNP VNFDSVFNRS RHTWSWGSPD ILPMFQHGAV PGRVDAFAYG
AELEDFSKDA TELDYWVFDH VKDFFAAAAT NETLNTALRE DKVVFFLHLL GLDTTGHSYR
PYSKEYLHNI KVVDQGVKEI VELIERFYGD DRTAFVFTAD HGMSDWGSHG DGHPNNTRTP
LISWGSGVAA PELHPGSIAP GHDELSSDWN LDHVRRHDVA QADVAALMSY LIGTEFPANG
VGQLPLNFLS ASIKEKAEAS LANAQVILEQ YRVKEENKRN VELRYQPYGQ LSDGNLDPES
RISHIRSLIE AGSFEEAIEE SDALMSIGLQ GLRYLQTYDW LFLRALITIG YLGWMAYATT
TVLSLYVVKE SMSPQRTLLG SAFFLSLLVA LYSSFIISKS PPAYYLYAFF PVLFWEEVYA
RRANVAKGFQ ALFGHVKSGG AVVALVFNVV LYLGVIQSLA LAYIHREILT GLFVLGAFWP
MTQGISFLRS HLFLSMLWFF SCLAMSTFTL LPAMKVEDIP LIMAGGGLMT FVGLAYLVLE
DFILSDVSSS KTKLKRLHTS RTLLGIQVGL IILAMLVTHS SATSLQAKLG LPKGNQIVGW
FVLVTSLLMP LAYRLQPNSH YMHRLAIIFL TCAPTFVILT ISYEGLFYVA FSITLLSWVR
LEYAVDAFTQ EKAKKQATVA GSQQHTPSTF RPLSLSDARI ALFFMVLLQS AFFSTGNIAS
ISSFSLESVS RLIPVFDPFS QGALLILKII IPFFLISANL GVLNKRLGVA PSAIFMVVLT
ASDVLTLYFF WVVKDEGSWL EIGSTITHFA IASFLCVFVA ALEFVSAAFI AGIEVEDTKS
AALTSASTKA DEKVPPVAGA E
