MCD4_CHAGB
ID MCD4_CHAGB Reviewed; 921 AA.
AC Q2H0X9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; ORFNames=CHGG_04567;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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; CH408032; EAQ87948.1; -; Genomic_DNA.
DR RefSeq; XP_001223781.1; XM_001223780.1.
DR AlphaFoldDB; Q2H0X9; -.
DR STRING; 38033.XP_001223781.1; -.
DR EnsemblFungi; EAQ87948; EAQ87948; CHGG_04567.
DR GeneID; 4391572; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q2H0X9; -.
DR OMA; TISHFCI; -.
DR OrthoDB; 270107at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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..921
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246205"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 715..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 921 AA; 101802 MW; 285252B2C2D957E8 CRC64;
MASFPRFRFL AIAVVFHLVK ASVDPTTRRS SSALRRPGHV ALIAGLYEDV SAVTTGWKLN
PVNFDSVFNR SRHTWSWGSP DILPMFEQGA VPGRVDAYTY GAELEDFSLD GFALDLWVFD
HVKELFAEAR TNKTLNDALR QDRIVFFLHL LGLDTTGHSF RPYSKEYLNN IKVVDKGVQE
ITELMKDFYA DDRTAFVFTA DHGMSDWGNH GDGHPDNTRT PLIAWGSGVA KPQLYPGEVA
PGHDEYSSDW NLDHIRRHDV EQADVAALMA YLAGTEFPAN SVGELPLSFL TAGLKEKAEA
SLVNAQGILE QYRVKEEGKK LTELRYRPYE PLSDEGMATE SRVAHIRQLI ETGSYEEAIE
ESAALLKVGL GGLRYLQTYD WLFLRALITI GYLGWVAYAL TTVIDLHVLH GRIQPSRTLI
GTIISTSALT ALYASFAISK SPLTYYAYAF FPVFFWEEVY ARRESLTEGR KELFGHIKSS
SNFVSLVFNC AVYVGIIESL ALGYIHREIL TILFVIGAFW PIAYGFSFLR QHMALSITWF
LSCIAMSTFT LLPPAMTTED VNMIMLGGAL MVLVGIIYLI LEDFVLSDFG WSEKPSSPRN
HVSRTLVGIQ IGLTLLAALV TRSSALSMQA NQGLPRGNQV MGWVVLVVSL LMPLAYRAKP
NNHYMHRILV IFLTCAPTFV ILTISYEGLF YIAFSAVLVS WVRLEHAIYK FPSSSANGAA
RSAPSPAKPH NLETSQTLPS PFRPLTLRDA RVALFFFVLF QAAFFSTGNV ASVSSFSLDS
VSRLIPIFDP FSQGAMLILK LLIPFALISA NLGILNKRLG VAPSALFMVV MAISDILTLY
FFWVVKDEGS WLEIGSTISH FVIASLLCVF VAALEGVSAM FIAGVEVSED VDRAVGKGAV
AEVLLEKTEA ERDGGAGSGG K
