ID   GPT_MOUSE               Reviewed;         410 AA.
AC   P42867; Q921W5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   24-JAN-2024, entry version 169.
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 {ECO:0000312|MGI:MGI:1196396}; Synonyms=Dpagt2, Gnpta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=1323278; DOI=10.1042/bj2850985;
RA   Rajput B., Ma J., Muniappa N., Schantz L., Naylor S.L., Lalley P.A.,
RA   Vijay I.K.;
RT   "Mouse UDP-GlcNAc: dolichyl-phosphate N-
RT   acetylglucosaminephosphotransferase. Molecular cloning of the cDNA,
RT   generation of anti-peptide antibodies and chromosomal localization.";
RL   Biochem. J. 285:985-992(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   STRAIN=BALB/cJ, and NIH Swiss; TISSUE=Liver, and Mammary gland;
RX   PubMed=8043075; DOI=10.1016/s0021-9258(17)36922-3;
RA   Rajput B., Ma J., Vijay I.K.;
RT   "Structure and organization of mouse GlcNAc-1-phosphate transferase gene.";
RL   J. Biol. Chem. 269:9590-9597(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10536042; DOI=10.1093/glycob/9.11.1263;
RA   Marek K.W., Vijay I.K., Marth J.D.;
RT   "A recessive deletion in the GlcNAc-1-phosphotransferase gene results in
RT   peri-implantation embryonic lethality.";
RL   Glycobiology 9:1263-1271(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- DEVELOPMENTAL STAGE: Highest activity is during the mid-phase of
CC       lactation.
CC   -!- RNA EDITING: Modified_positions=74 {ECO:0000269|PubMed:8043075};
CC       Note=Partially edited.;
CC   -!- DISRUPTION PHENOTYPE: Mice die 4 to 5 days post-fertilization, just
CC       after implantation, suggesting that protein function and N-
CC       glycosylation are essential in early embryogenesis.
CC       {ECO:0000269|PubMed:10536042}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
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DR   EMBL; X65603; CAA46553.1; -; mRNA.
DR   EMBL; BC010474; AAH10474.1; -; mRNA.
DR   CCDS; CCDS23104.1; -.
DR   PIR; S24326; S24326.
DR   RefSeq; NP_031901.2; NM_007875.2.
DR   PDB; 6JQ2; X-ray; 2.40 A; P=206-213.
DR   PDBsum; 6JQ2; -.
DR   AlphaFoldDB; P42867; -.
DR   SMR; P42867; -.
DR   BioGRID; 199296; 1.
DR   IntAct; P42867; 1.
DR   STRING; 10090.ENSMUSP00000056282; -.
DR   GlyCosmos; P42867; 1 site, No reported glycans.
DR   GlyGen; P42867; 1 site.
DR   iPTMnet; P42867; -.
DR   PhosphoSitePlus; P42867; -.
DR   EPD; P42867; -.
DR   jPOST; P42867; -.
DR   MaxQB; P42867; -.
DR   PaxDb; 10090-ENSMUSP00000056282; -.
DR   PeptideAtlas; P42867; -.
DR   ProteomicsDB; 269626; -.
DR   Antibodypedia; 32608; 172 antibodies from 24 providers.
DR   DNASU; 13478; -.
DR   Ensembl; ENSMUST00000054708.5; ENSMUSP00000056282.4; ENSMUSG00000032123.6.
DR   GeneID; 13478; -.
DR   KEGG; mmu:13478; -.
DR   UCSC; uc009pcv.1; mouse.
DR   AGR; MGI:1196396; -.
DR   CTD; 1798; -.
DR   MGI; MGI:1196396; Dpagt1.
DR   VEuPathDB; HostDB:ENSMUSG00000032123; -.
DR   eggNOG; KOG2788; Eukaryota.
DR   GeneTree; ENSGT00390000011424; -.
DR   HOGENOM; CLU_029942_0_1_1; -.
DR   InParanoid; P42867; -.
DR   OMA; LPHFNAR; -.
DR   OrthoDB; 5481729at2759; -.
DR   PhylomeDB; P42867; -.
DR   TreeFam; TF313734; -.
DR   Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 13478; 30 hits in 82 CRISPR screens.
DR   ChiTaRS; Dpagt1; mouse.
DR   PRO; PR:P42867; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P42867; Protein.
DR   Bgee; ENSMUSG00000032123; Expressed in yolk sac and 219 other cell types or tissues.
DR   ExpressionAtlas; P42867; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IDA:MGI.
DR   GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; ISS:MGI.
DR   GO; GO:0019348; P:dolichol metabolic process; ISO:MGI.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; ISO:MGI.
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.
DR   Genevisible; P42867; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Magnesium; Membrane; Metal-binding; Reference proteome; RNA editing;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT                   acetylglucosaminephosphotransferase"
FT                   /id="PRO_0000108762"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        11..40
FT                   /note="Helical; Name=Helix 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        41..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        61..80
FT                   /note="Helical; Name=Helix 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        81..93
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        94..120
FT                   /note="Helical; Name=Helix 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        121..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        124..145
FT                   /note="Helical; Name=Helix 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        146..168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        169..188
FT                   /note="Helical; Name=Helix 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        189..194
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        195..215
FT                   /note="Helical; Name=Helix 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        216..220
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        221..244
FT                   /note="Helical; Name=Helix 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        245..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..271
FT                   /note="Helical; Name=Helix 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        272..273
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        274..295
FT                   /note="Helical; Name=Helix 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        296..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        378..402
FT                   /note="Helical; Name=Helix 10"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   TOPO_DOM        403..410
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   BINDING         46..48
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         58
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         127
FT                   /ligand="dolichyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57683"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         180..188
FT                   /ligand="dolichyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57683"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         193
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   BINDING         303..305
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         74
FT                   /note="C -> Y (in RNA edited version)"
SQ   SEQUENCE   410 AA;  46412 MW;  F729D6983FA67E0B CRC64;
     MWAFPELPLP LPLLVNLIGS LLGFVATVTL IPAFRSHFIA ARLCGQDLNK LSQQQIPESQ
     GVISGAVFLI ILFCFIPFPF LNCFVEEQCK AFPHHEFVAL IGALLAICCM IFLGFADDVL
     NLRWRHKLLL PTAASLPLLM VYFTNFGNTT IVVPKPFRWI LGLHLDLGIL YYVYMGLLAV
     FCTNAINILA GINGLEAGQS LVISASIIVF NLVELEGDYR DDHIFSLYFM IPFFFTTLGL
     LYHNWYPSRV FVGDTFCYFA GMTFAVVGIL GHFSKTMLLF FMPQVFNFLY SLPQLFHIIP
     CPRHRMPRLN AKTGKLEMSY SKFKTKNLSF LGTFILKVAE NLRLVTVHQG ESEDGAFTEC
     NNMTLINLLL KVFGPIHERN LTLLLLLLQV LSSAATFSIR YQLVRLFYDV
//