ID   GPT_CRIGR               Reviewed;         408 AA.
AC   P24140; G3I967;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE            EC=2.7.8.15 {ECO:0000269|PubMed:1700792, ECO:0000269|PubMed:7772861};
DE   AltName: Full=GlcNAc-1-P transferase;
DE            Short=G1PT;
DE            Short=GPT;
DE   AltName: Full=N-acetylglucosamine-1-phosphate transferase;
GN   Name=DPAGT1; Synonyms=DPAGT2, GNPTA, GTR2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   TISSUE=Ovary;
RX   PubMed=1700792; DOI=10.1016/s0021-9258(17)30548-3;
RA   Scocca J.R., Krag S.S.;
RT   "Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-D-
RT   glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase
RT   from Chinese hamster ovary cells.";
RL   J. Biol. Chem. 265:20621-20626(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=7772861; DOI=10.1093/glycob/5.1.129;
RA   Scocca J.R., Zou J., Krag S.S.;
RT   "Genomic organization and expression of hamster UDP-N-
RT   acetylglucosamine:dolichyl phosphate N-acetylglucosaminyl phosphoryl
RT   transferase.";
RL   Glycobiology 5:129-136(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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:0000269|PubMed:1700792, ECO:0000269|PubMed:7772861}.
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; Evidence={ECO:0000269|PubMed:1700792,
CC         ECO:0000269|PubMed:7772861};
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:0000269|PubMed:1700792, ECO:0000269|PubMed:7772861}.
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; M36899; AAA37027.1; -; mRNA.
DR   EMBL; U15161; AAA51872.1; -; Genomic_DNA.
DR   EMBL; U09453; AAA85220.1; -; Genomic_DNA.
DR   EMBL; JH001575; EGV99104.1; -; Genomic_DNA.
DR   RefSeq; NP_001230970.1; NM_001244041.1.
DR   AlphaFoldDB; P24140; -.
DR   SMR; P24140; -.
DR   GlyCosmos; P24140; 1 site, No reported glycans.
DR   PaxDb; 10029-NP_001230970-1; -.
DR   Ensembl; ENSCGRT00000008114; ENSCGRP00000007981; ENSCGRG00000005819.
DR   Ensembl; ENSCGRT00001005610.1; ENSCGRP00001003822.1; ENSCGRG00001004728.1.
DR   Ensembl; ENSCGRT00015024020; ENSCGRP00015019491; ENSCGRG00015014973.
DR   GeneID; 100689054; -.
DR   KEGG; cge:100689054; -.
DR   CTD; 1798; -.
DR   eggNOG; KOG2788; Eukaryota.
DR   GeneTree; ENSGT00390000011424; -.
DR   InParanoid; G3I967; -.
DR   OMA; LPHFNAR; -.
DR   OrthoDB; 5481729at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI: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; IMP:UniProtKB.
DR   GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IEA:Ensembl.
DR   GO; GO:0019408; P:dolichol biosynthetic process; IMP: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   1: Evidence at protein 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_0000108760"
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"
SQ   SEQUENCE   408 AA;  46250 MW;  CB0FF5946C07BEF3 CRC64;
     MWAFPELPLP LLVNLFGSLL GFVATVTLIP AFRSHFIAAR LCGQDLNKLS RQQIPESQGV
     ICGAVFLIIL FCFIPFPFLN CFVEEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
     RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRWILG LHLDLGILYY VYMGLLAVFC
     TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDYRDD HVFSLYFMIP FFFTTLGLLY
     HNWYPSQVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFI PQVFNFLYSL PQLLHAIPCP
     RHRIPRLNPK TGKLEMSYSK FKTKNLSFLG TFILKVAERL QLVTVHRGES EDGAFTECNN
     MTLINLLLKI FGPIHERNLT LLLLLLQILS SAVTFSIRYQ LVRLFYDV
//