ID   B3KY32_HUMAN            Unreviewed;       408 AA.
AC   B3KY32;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JUL-2024, entry version 54.
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 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: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}.
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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
//