MCD4_ASPFU
ID MCD4_ASPFU Reviewed; 1032 AA.
AC Q4W9R7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
DE AltName: Full=AfpigN;
GN Name=mcd4; Synonyms=pigN; ORFNames=AFUA_4G03970;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=YJ-407;
RA Ouyang H., Jin C.;
RT "Phosphoethanolamine transferases gene, AfpigN, which is involved in the
RT biosynthesis of glycosylphosphatidylinositol in Aspergillus fumigatus
RT YJ407.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; DQ426542; ABD84043.1; -; mRNA.
DR EMBL; AAHF01000016; EAL84546.1; -; Genomic_DNA.
DR RefSeq; XP_746584.1; XM_741491.1.
DR AlphaFoldDB; Q4W9R7; -.
DR SMR; Q4W9R7; -.
DR STRING; 746128.CADAFUBP00009624; -.
DR PRIDE; Q4W9R7; -.
DR EnsemblFungi; EAL84546; EAL84546; AFUA_4G03970.
DR GeneID; 3503916; -.
DR KEGG; afm:AFUA_4G03970; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q4W9R7; -.
DR OMA; TISHFCI; -.
DR OrthoDB; 270107at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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: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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1032
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246201"
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..468
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..523
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..596
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..647
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..722
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..841
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..914
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..935
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..1032
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 994..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1032 AA; 114174 MW; 5F458EDCDFD07863 CRC64;
MARLGRFGFL ALAVVFHLIY AYSIFDIYFV SPIVSGMRSY GVEREPGAKA PASRLVLFVA
DGLRADKAFQ PAPDPSPEDG EDAENNDPIY LAPFIRSRVL SHGTFGVSHT RVPTESRPGH
VALIAGLYED VSAVTTGWKL NPVNFDSVFN QSRHTWSWGS PDILAMFKEG AVPGRVDADM
YGEEIEDFTM DATQLDTWVF NKVKELFASA KSDPELDAKL RQDKVVFFLH LLGLDTTGHG
YRPYSREYLH NIKIVDKGVQ EIATLIEEFY GDDRTAFVFT ADHGMSDWGS HGDGHPDNTR
TPLVVWGSGV AGPKYTDGKA VTGHEDGFSA DWGLDGIQRH DVAQADVAAL MAYLAGLDFP
VNSVGQLPLE YIDASPKEKA LAALANTQEV LEMYRVKEAQ KRAALLRYKP FEPLADHGKN
SVEEHIAEIQ VLIANGSYDE PIKRSGALFA TALEGLRYLQ TYDWLFLRTI ITFGYLGWIA
YALTTVIDLH VLHRTSDSKR TVGSTIFFTS ILAALFSVLL YQKSSWQYYV YGAFPIFFWE
EVFARRKALI AGREILLGHV RSFGGYIASG FQLVAFVAVL EALLMRHQVQ SYFHREIYTV
CFVLGSFWPI LYGVDFVRQN TVLSATWAVG CSLMSTFTLL PVIKVENINT ITYGALLMFF
TGLFYLLFED TILKHSKSSG HAPGAISSLG SRVIMGMQVG MVLLALIVTR SSVSSLQAKQ
GLPFGNQVVG WFVLVASLVL PFFHRLYPNS HYLHRLMVLF LTFSPTFIIL TISYEGLFYF
VFCMTLVTWV RLEHAIYVYT ARSSAHYGGN NTVPKKPGLN ATAVIDGQEY RYRRLGLADT
RVALFFFFLL QSAFFSTGNI ASVSSFSLES VFRLIPVFSP FSQSALLILK LLIPFAIISA
NLGILNRRLE VAPSALFMVV MSISDVMTLN FFYMVRDEGS WLDIGTTISH FLIASFLCTF
VAGLEFLSEV FISGVDFGPT TKAIGASITK TVGGTAGSDV VDSQSGPEDA ANSKKAEGLE
GSETIRQNGG SV
