ID B3KY32_HUMAN Unreviewed; 408 AA. AC B3KY32; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 03-AUG-2022, entry version 48. DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659}; DE EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225}; DE AltName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00029567}; DE AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00033238}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG54694.1}; RN [1] {ECO:0000313|EMBL:BAG54694.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Trachea {ECO:0000313|EMBL:BAG54694.1}; RA Kanehori K., Ishibashi T., Chiba Y., Fujimori K., Hiraoka S., Tanai H., RA Watanabe S., Ishida S., Ono Y., Hotuta T., Watanabe M., Sugiyama T., RA Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J., RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Matsuo K., RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., RA Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y., RA Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.; RT "NEDO human cDNA sequencing project."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. 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=a 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; AK128572; BAG54694.1; -; mRNA. DR PeptideAtlas; B3KY32; -. 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. 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; 1. DR Pfam; PF00953; Glycos_transf_4; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAG54694.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 60..83 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 95..114 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..189 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 195..211 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 223..243 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 249..271 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 379..401 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 408 AA; 46118 MW; 627087E6DCE7AB45 CRC64; MWAFSELPMP LLINLIVSLL GFVATVTLIP AFRGHFIAAR LCGQDLNKTS RQQIPESQGV ISGAVFLIIL FCFIPFPFLN CFVKEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRPILG LHLDLGILYY VYMGLLAVFC TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDCRDD HVFSLYFMIP FFFTTLGLLY HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP RHRIPRLNIK TGKLEMSYSK FRTKSLSFLG TFILKVAESL QLVTVHQSET EDGEFTECNN MTLINLLLKV LGPIHERNLT LLLLLLQILG SAITFSIRYQ LVRLFYDV //