GPT_MOUSE
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 03-AUG-2022, entry version 161.
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 IntAct; P42867; 1.
DR STRING; 10090.ENSMUSP00000056282; -.
DR GlyGen; P42867; 1 site.
DR iPTMnet; P42867; -.
DR PhosphoSitePlus; P42867; -.
DR EPD; P42867; -.
DR jPOST; P42867; -.
DR MaxQB; P42867; -.
DR PaxDb; P42867; -.
DR PeptideAtlas; P42867; -.
DR PRIDE; P42867; -.
DR ProteomicsDB; 269626; -.
DR Antibodypedia; 32608; 158 antibodies from 23 providers.
DR DNASU; 13478; -.
DR Ensembl; ENSMUST00000054708; ENSMUSP00000056282; ENSMUSG00000032123.
DR GeneID; 13478; -.
DR KEGG; mmu:13478; -.
DR UCSC; uc009pcv.1; mouse.
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; LVWMGPM; -.
DR OrthoDB; 1079130at2759; -.
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 77 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 216 other tissues.
DR ExpressionAtlas; P42867; baseline and differential.
DR Genevisible; P42867; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
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; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
DR PANTHER; PTHR10571; PTHR10571; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
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
