GPI19_ASHGO
ID GPI19_ASHGO Reviewed; 153 AA.
AC Q756D4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19;
DE EC=2.4.1.198;
GN Name=GPI19; OrderedLocusNames=AER333C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Part of the complex catalyzing the transfer of N-
CC acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol,
CC the first step of GPI biosynthesis. Involved in cell wall biosynthesis
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Component of the phosphatidylinositol N-
CC acetylglucosaminyltransferase complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPI19 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS53013.1; -; Genomic_DNA.
DR RefSeq; NP_985189.1; NM_210543.1.
DR AlphaFoldDB; Q756D4; -.
DR SMR; Q756D4; -.
DR STRING; 33169.AAS53013; -.
DR EnsemblFungi; AAS53013; AAS53013; AGOS_AER333C.
DR GeneID; 4621402; -.
DR KEGG; ago:AGOS_AER333C; -.
DR eggNOG; KOG2257; Eukaryota.
DR HOGENOM; CLU_081616_4_0_1; -.
DR InParanoid; Q756D4; -.
DR OMA; RYWIICI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:EnsemblFungi.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR013717; PIG-P.
DR InterPro; IPR016542; PIG-P_GPI19.
DR Pfam; PF08510; PIG-P; 1.
DR PIRSF; PIRSF008765; PIG-P_GPI19; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit GPI19"
FT /id="PRO_0000240379"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..67
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 17597 MW; 685A221FCD2FB56F CRC64;
MKQDKRKYSG FVQSVGITCV LILIILWTLL PYPLLDPEKR LAEPQTTTES ISLFLDELVE
LFPQRYWIIC IQCMILMDML FVYIGLPIFN QSVLTVRLDD LRTITDSKAS VVMCESHAEF
LTSYAHTETS GVYDLPITEV SRLLYGKARH KSD
