MCD4_ASPOR
ID MCD4_ASPOR Reviewed; 1022 AA.
AC Q2U0S9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=mcd4; ORFNames=AO090011000320;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007171; BAE64836.1; -; Genomic_DNA.
DR RefSeq; XP_001825969.1; XM_001825917.1.
DR AlphaFoldDB; Q2U0S9; -.
DR SMR; Q2U0S9; -.
DR STRING; 510516.Q2U0S9; -.
DR EnsemblFungi; BAE64836; BAE64836; AO090011000320.
DR GeneID; 5998072; -.
DR KEGG; aor:AO090011000320; -.
DR VEuPathDB; FungiDB:AO090011000320; -.
DR HOGENOM; CLU_007676_0_0_1; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000006564; Chromosome 7.
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: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; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 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..1022
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246202"
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..466
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..560
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..614
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..685
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..749
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..837
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 859..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..910
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..1022
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 998..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1022 AA; 113035 MW; E21FDA3B26963252 CRC64;
MARVGRVGFL TLAVVFHLMY AYSIFDIYFV SPIVSGMRSF GVEREASAEA PAKRLVLFVA
DGLRADKAFQ ALPDPDAPSD LENDEPIYLA PFIRSRALSH GTFGISHTRV PTESRPGHVA
LIAGLYEDVS AVTTGWKLNP VDFDSVFNRS RHTWSWGSPD ILPMFKEGAV PGRIDADTYG
EEAEDFSADA TKLDIWVFDK VKELFASAKK DPELDAKLRE DKLVFFLHLL GLDTTGHAYR
PYSKEYLRNI KLVDKGVQEI TQLVEDFYGD GKTSFVFTAD HGMSDWGSHG DGHPDNTRTP
LVVWGSGVAS PRYTHEGTIT GHEDGVSADW GLDSVQRNDV AQADVAALMA YLVGLDFPTN
SVGQLPLGYL DTSPKDKALA ALANAQGVLE MYRVKEEQKR DALLRYTPFE PLADNGETSV
EARLERIKTL ISNKSYDASI QLSSELLLTA LEGLRYLQTY DWLFLRTIVS LGYLGWIAYA
LTTVIDLHVL HGKSESNRTT FSIMFFSSIL VALFSVLLYQ GSSWRYYLYA LFPIFFWEEV
FARRKALLAG REILLGHVHS VSGYFAFAIQ LLLYVGVLEA LVQSYFHRDI FTVCFILGGF
WPITYGTKFL GQHKLLSASW ALGCFLMSIF TLLPANKVED MMMISCGSLL MFLTGLLYLI
FERSILGQKR SSDPNSVVSS CGSRTIMGAQ VGMILLALIV TRSSVASLQA KQGLPLGNQV
LGWAILVSSL LLPFLHRLYP NSHYLHRLMV IFLTFSPIFI ILTISYEGLF YFVFCMTLLA
WVRLEQAIYI HTTAPTREQD HSVANGSLPA KKPSPGNTVV VEGQPYRYRT LSVSDARVAL
FFFFLLQSGF FSTGNIASVS SFSLDSVYRL IPIFNPFAQG ALLILKLLIP FAIISANLGI
LNHRLEVAPS ALFMVVMSIS DVMTLNFFYM VRDEGSWLEI GTTISHFCIA SFLCTFVAVL
EFLSELFISG VDFGHPATTV GSAVAKAVNG SVACGHSPDS DISGEDSTSV GITAKADPDA
RS
