ID   GPT_BOVIN               Reviewed;         408 AA.
AC   Q5EA65; Q3T0F3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE            EC=2.7.8.15 {ECO:0000250|UniProtKB:Q9H3H5};
DE   AltName: Full=GlcNAc-1-P transferase;
DE            Short=G1PT;
DE            Short=GPT;
DE   AltName: Full=N-acetylglucosamine-1-phosphate transferase;
GN   Name=DPAGT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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:0000250|UniProtKB:Q9H3H5}.
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:0000250|UniProtKB:Q9H3H5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9H3H5};
CC   -!- ACTIVITY REGULATION: Activated by mannosylphosphoryldolichol and
CC       phospholipids such as phosphatidylglycerol and phosphatidylcholine.
CC       Inhibited by natural nucleoside antibiotic tunicamycin, which acts as a
CC       structural analog and competitor of UDP-GlcNAc.
CC       {ECO:0000250|UniProtKB:Q9H3H5}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9H3H5}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9H3H5}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9H3H5}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9H3H5}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
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DR   EMBL; BT020704; AAX08721.1; -; mRNA.
DR   EMBL; BC102417; AAI02418.1; -; mRNA.
DR   RefSeq; NP_001015664.1; NM_001015664.1.
DR   AlphaFoldDB; Q5EA65; -.
DR   SMR; Q5EA65; -.
DR   STRING; 9913.ENSBTAP00000072144; -.
DR   GlyCosmos; Q5EA65; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000007065; -.
DR   GeneID; 537812; -.
DR   KEGG; bta:537812; -.
DR   CTD; 1798; -.
DR   eggNOG; KOG2788; Eukaryota.
DR   HOGENOM; CLU_029942_0_1_1; -.
DR   InParanoid; Q5EA65; -.
DR   TreeFam; TF313734; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; ISS:UniProtKB.
DR   GO; GO:0019408; P:dolichol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
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; Glycoprotein; Glycosyltransferase; Magnesium;
KW   Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..408
FT                   /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT                   acetylglucosaminephosphotransferase"
FT                   /id="PRO_0000314781"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        11..38
FT                   /note="Helical; Name=Helix 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        39..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        59..78
FT                   /note="Helical; Name=Helix 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        79..91
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        92..118
FT                   /note="Helical; Name=Helix 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        119..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        122..143
FT                   /note="Helical; Name=Helix 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        144..166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        167..186
FT                   /note="Helical; Name=Helix 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        187..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        193..213
FT                   /note="Helical; Name=Helix 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        214..218
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        219..242
FT                   /note="Helical; Name=Helix 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        243..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        251..269
FT                   /note="Helical; Name=Helix 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        270..271
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        272..293
FT                   /note="Helical; Name=Helix 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        294..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        376..400
FT                   /note="Helical; Name=Helix 10"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        401..408
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   BINDING         44..46
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         56
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         125
FT                   /ligand="dolichyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57683"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         178..186
FT                   /ligand="dolichyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57683"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         191
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         301..303
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        312
FT                   /note="G -> D (in Ref. 2; AAI02418)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  46045 MW;  9BD875493287FB1C CRC64;
     MWAFPELPMP LLVNLIGSLM GFVATVTLIP AFRGHFIAAR LCGQDLNKSS REQIPESQGV
     ISGAVFLIIL FCFIPFPFLN CFVEQQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
     RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPLRPILG LHLDLGILYY VYMGLLAVFC
     TNAINILAGI NGLEAGQSLV ISASIIVFNL VELDGDYRDD HIFSLYFMIP FFFTTLGLLY
     HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP
     RHRMPRLNTK TGKLEMSYSK FKTKSLSFLG TFILKVAENL GLLTVRHSED EDGAFTECNN
     MTLINLLLKV FGPMHERNLT LLLLLLQVVG SAVTFSIRYQ LVRLFYDV
//