ID A0A095AEX1_SCHHA Unreviewed; 423 AA. AC A0A095AEX1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 02-DEC-2020, entry version 27. DE RecName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00013408}; DE EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225}; DE AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00013705}; DE AltName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659}; GN ORFNames=MS3_00550 {ECO:0000313|EMBL:KGB32396.1}; OS Schistosoma haematobium (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB32396.1}; RN [1] {ECO:0000313|EMBL:KGB32396.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22246508; DOI=10.1038/ng.1065; RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y., RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G., RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A., RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J., RA Wang J., Gasser R.B.; RT "Whole-genome sequence of Schistosoma haematobium."; RL Nat. Genet. 44:221-225(2012). CC -!- FUNCTION: Catalyzes the initial step of dolichol-linked oligosaccharide CC biosynthesis in N-linked protein glycosylation pathway: transfers CC GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate CC (P-dolichol), yielding GlcNAc-P-P-dolichol. CC {ECO:0000256|ARBA:ARBA00003598}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N- CC acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP; CC Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519, CC ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, CC ChEBI:CHEBI:58427; EC=2.7.8.15; CC Evidence={ECO:0000256|ARBA:ARBA00000093}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. CC {ECO:0000256|ARBA:ARBA00009317}. 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; KL250502; KGB32396.1; -; Genomic_DNA. DR RefSeq; XP_012792193.1; XM_012936739.1. DR GeneID; 24588365; -. DR KEGG; shx:MS3_00550; -. DR CTD; 24588365; -. DR OrthoDB; 1079130at2759; -. DR UniPathway; UPA00378; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro. DR CDD; cd06855; GT_GPT_euk; 1. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR033895; GPT. DR PANTHER; PTHR10571; PTHR10571; 2. DR Pfam; PF00953; Glycos_transf_4; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGB32396.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 20..38 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 72..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 136..165 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 177..197 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 209..235 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 241..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 395..418 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 329..361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..355 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 423 AA; 47134 MW; 3AC3D0D8716CED69 CRC64; MESTCASTNE GHLLSTYRHF FELLVLVCMS IFGAKYVLKL FKKYKGEFLR AGFAGVDMNK PSKPTLPEAQ GVICGVVFLS IMFLFIPVPF WRYLVGKADA QSLEFIQFLA GLLSICCMLF LGFADDALNL PWRHKIGFPF VAGLPLLMVY LANEGTTSIA VPVMLRNALG SSVDIGILYY IYMGLLTVFC TNSINIYAGV NGLEVGQAIV IGASLILFNL IELSSMTFAV VGILGHFSKT LLLFFLPQIV NFLYSTPQLF GLIPCPRHRL PRYDPADGLL HPSRVRFHPK SLSRPGQFVL TVFSYVGIIE CKLCPDCIPN ISTSPTTGMI VSQSSHENMS SDEEQTSERQ RARSRSPAQT KLPTEEIVEV DNLTVINMML RVLGPRNEQQ TTNTLLLLQI LCSCFAFMIR YPLAWLFYDV PAK //