MCD4_NEUCR
ID MCD4_NEUCR Reviewed; 996 AA.
AC Q7SAP1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=mcd-4; ORFNames=B2N18.290, NCU07999;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX897674; CAE85530.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33433.1; -; Genomic_DNA.
DR RefSeq; XP_962669.1; XM_957576.2.
DR AlphaFoldDB; Q7SAP1; -.
DR SMR; Q7SAP1; -.
DR STRING; 5141.EFNCRP00000008276; -.
DR EnsemblFungi; EAA33433; EAA33433; NCU07999.
DR GeneID; 3878833; -.
DR KEGG; ncr:NCU07999; -.
DR VEuPathDB; FungiDB:NCU07999; -.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q7SAP1; -.
DR OMA; TISHFCI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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 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..996
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246210"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..463
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..518
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..586
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..637
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..715
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..822
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..895
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 917..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 933..953
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 954..996
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 996 AA; 110558 MW; 6F97742F48A94AEB CRC64;
MAAFPRFRFL AIAVIFHFAY IFSIFDIYFV SPIETGMRLF NVQRPPNRSA PADRLVLFVG
DGLRADKALQ SHPEPYPKSD ADLTPRPLAP YLRSKILEQG TFGVSHTRVP TESRPGHVAL
IAGLYEDVSA VTTGWKLNPV NFDSLFNRSR HTWSWGSPDI LPMFEQGAVP GRVDAYTYGH
EFEDFSSDAT QLDLWVFDHV KDFFAEARRN KTLAEALRQD KIVFFLHLLG LDTTGHSYRP
YSKEYLNNIK IVDQGVKEVA ELFRDFYRDG RTAFVFTADH GMSDWGSHGD GHPDNTRTPL
IVWGSGVAKP QLYPGEVAPG HDEYSADWNL DHVRRHDVAQ ADVAALMSYL VGVEFPANSV
GELPLSYLAA DIKEKAEASL VNVQGILEQY RVKEEKKKAT ELKYRPYQPF GENGLSPERR
VAEIRQLIDA GRYEEAIEES AALMKVGLGG LRYLQTYDWL FLRALITIGY LGWIAYALTT
VVDLHVLHGR VRPSRTLGGG LFFTSVLVAL YASLVISKSP LTYYVYAFFP VFFWEEVYAH
RESLAAGRKE LLGHINSGGS VASFVLNSAL YVGVIESLAL GYIHREILSV LFVLGSFWPF
THGLSFLKKH GALSATWFLA CIAMSTFTLL PAMKAENVNL ITIGGVLMVV IGLLYLIFED
FVLADFSWNA KPTSRNHLSR SLVGIQVGLT VLSIIITRSS ALSLQAKQGL PRGNQIMGWV
TLVASLLMPL AYRLRPNNHY MHRILVIFLT CAPTFVILTI SYEGLFYLVF SALLVSWVRL
EHAVQKFTSS KAPQTAATKK PTTTTESHLP APFRPLTLHD ARVALFFFIL LQSAFFSTGN
VASVSSFSLD SVYRLIPIFD PFSQGAMLIL KLMIPFALIS ANLGILNKRL GVAPSALFMV
VMGISDILTL YFFWVVKDEG SWLEIGSTIS HFVIASLLCV FVSALEPVSA AFIAGVEVGE
ESELKEEGKV AEKVVEKVNE AVEGLVSGGD GGGDES
