ID B3KY32_HUMAN Unreviewed; 408 AA. AC B3KY32; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 02-OCT-2024, entry version 55. 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: UDP-N-acetylglucosamine--dolichyl-phosphate N- CC acetylglucosaminephosphotransferase that operates in the biosynthetic CC pathway of dolichol-linked oligosaccharides, the glycan precursors CC employed in protein asparagine (N)-glycosylation. The assembly of CC dolichol-linked oligosaccharides begins on the cytosolic side of the CC endoplasmic reticulum membrane and finishes in its lumen. The CC sequential addition of sugars to dolichol pyrophosphate produces CC dolichol-linked oligosaccharides containing fourteen sugars, including CC two GlcNAcs, nine mannoses and three glucoses. Once assembled, the CC oligosaccharide is transferred from the lipid to nascent proteins by CC oligosaccharyltransferases. Catalyzes the initial step of dolichol- CC linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from CC cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P- CC dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic CC leaflet of the endoplasmic reticulum membrane. CC {ECO:0000256|ARBA:ARBA00044717}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-N-acetyl-alpha-D- CC glucosamine = an N-acetyl-alpha-D-glucosaminyl-diphospho-di- CC trans,poly-cis-dolichol + UMP; Xref=Rhea:RHEA:13289, Rhea:RHEA- CC COMP:19498, Rhea:RHEA-COMP:19507, ChEBI:CHEBI:57683, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:58427; EC=2.7.8.15; CC Evidence={ECO:0000256|ARBA:ARBA00044631}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13290; CC Evidence={ECO:0000256|ARBA:ARBA00044631}; 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. 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 AlphaFoldDB; B3KY32; -. DR PeptideAtlas; B3KY32; -. DR UniPathway; UPA00378; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016757; F:glycosyltransferase activity; 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; IPR048439; DPAGT1_ins. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR033895; GPT. DR PANTHER; PTHR10571; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR10571:SF0; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1. DR Pfam; PF21383; DPAGT1_ins; 1. DR Pfam; PF00953; Glycos_transf_4; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; 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" FT DOMAIN 318..360 FT /note="DPAGT1 insertion" FT /evidence="ECO:0000259|Pfam:PF21383" 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 //