GPT_CRILO
ID GPT_CRILO Reviewed; 408 AA.
AC P23338;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE EC=2.7.8.15 {ECO:0000269|PubMed:2167312};
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;
OS Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND PATHWAY.
RX PubMed=2167312; DOI=10.1016/s0021-9258(18)77293-1;
RA Zhu X., Lehrman M.A.;
RT "Cloning, sequence, and expression of a cDNA encoding hamster UDP-
RT GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase.";
RL J. Biol. Chem. 265:14250-14255(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 248-271.
RX PubMed=2848842; DOI=10.1016/s0021-9258(19)77705-9;
RA Lehrman M.A., Zhu X., Khounlo S.;
RT "Amplification and molecular cloning of the hamster tunicamycin-sensitive
RT N-acetylglucosamine-1-phosphate transferase gene. The hamster and yeast
RT enzymes share a common peptide sequence.";
RL J. Biol. Chem. 263:19796-19803(1988).
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:2167312}.
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:0000269|PubMed:2167312};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H3H5};
CC -!- ACTIVITY REGULATION: Inhibited by natural nucleoside antibiotic
CC tunicamycin, which acts as a structural analog and competitor of UDP-
CC GlcNAc. {ECO:0000269|PubMed:2167312}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:2167312}.
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; J05590; AAA36965.1; -; mRNA.
DR PIR; A37813; A37813.
DR AlphaFoldDB; P23338; -.
DR SMR; P23338; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
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 Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Membrane; Metal-binding; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108759"
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; 46191 MW; 108C4D7598B8F4F3 CRC64;
MWAFPELPLP LLVNLFGSLL GFVATVTLIP AFRSHFIAAR LCGQDLNKLS RQQIPESQGV
ICGAVFLIIL FCFIPFPFLN CFVEEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
PWRHKLLLPT 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
