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-APR-2013, entry version 104.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE EC=2.7.8.15;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=1323278;
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/c, and NIH Swiss; TISSUE=Liver, and Mammary gland;
RX PubMed=8043075;
RA Rajput B., Ma J., Vijay I.K.;
RT "Structure and organization of mouse GlcNAc-1-phosphate transferase
RT 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
RT project: 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
RT in peri-implantation embryonic lethality.";
RL Glycobiology 9:1263-1271(1999).
CC -!- FUNCTION: Catalyzes the initial step in the synthesis of dolichol-
CC P-P-oligosaccharides.
CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + dolichyl
CC phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.
CC -!- ENZYME REGULATION: Enzyme activity is stimulated by
CC phosphatidylglycerol and mannosylphosphoryldolichol and inhibited
CC by tunicamycin.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- DEVELOPMENTAL STAGE: Highest activity is during the mid-phase of
CC lactation.
CC -!- RNA EDITING: Modified_positions=74; Note=Partially edited.
CC -!- DISRUPTION PHENOTYPE: Mice die 4 to 5 days post-fertilization,
CC just after implantation, suggesting that protein function and N-
CC glycosylation are essential in early embryogenesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
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DR EMBL; X65603; CAA46553.1; -; mRNA.
DR EMBL; BC010474; AAH10474.1; -; mRNA.
DR IPI; IPI00120705; -.
DR PIR; S24326; S24326.
DR RefSeq; NP_031901.2; NM_007875.2.
DR UniGene; Mm.18353; -.
DR PhosphoSite; P42867; -.
DR PaxDb; P42867; -.
DR PRIDE; P42867; -.
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 eggNOG; COG0472; -.
DR GeneTree; ENSGT00390000011424; -.
DR HOGENOM; HOG000163915; -.
DR HOVERGEN; HBG000846; -.
DR InParanoid; P42867; -.
DR KO; K01001; -.
DR OMA; PFLNCFV; -.
DR OrthoDB; EOG4868CQ; -.
DR UniPathway; UPA00378; -.
DR ChiTaRS; DPAGT1; mouse.
DR NextBio; 283963; -.
DR ArrayExpress; P42867; -.
DR Bgee; P42867; -.
DR Genevestigator; P42867; -.
DR GermOnline; ENSMUSG00000032123; Mus musculus.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:MGI.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; 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:0019408; P:dolichol biosynthetic process; IEA:Compara.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:Compara.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:Compara.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; RNA editing;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 410 UDP-N-acetylglucosamine--dolichyl-
FT phosphate N-
FT acetylglucosaminephosphotransferase.
FT /FTId=PRO_0000108762.
FT TOPO_DOM 1 6 Lumenal (Potential).
FT TRANSMEM 7 34 Helical; (Potential).
FT TOPO_DOM 35 59 Cytoplasmic (Potential).
FT TRANSMEM 60 81 Helical; (Potential).
FT TOPO_DOM 82 96 Lumenal (Potential).
FT TRANSMEM 97 116 Helical; (Potential).
FT TOPO_DOM 117 127 Cytoplasmic (Potential).
FT TRANSMEM 128 147 Helical; (Potential).
FT TOPO_DOM 148 166 Lumenal (Potential).
FT TRANSMEM 167 186 Helical; (Potential).
FT TOPO_DOM 187 196 Cytoplasmic (Potential).
FT TRANSMEM 197 213 Helical; (Potential).
FT TOPO_DOM 214 223 Lumenal (Potential).
FT TRANSMEM 224 242 Helical; (Potential).
FT TOPO_DOM 243 254 Cytoplasmic (Potential).
FT TRANSMEM 255 271 Helical; (Potential).
FT TOPO_DOM 272 276 Lumenal (Potential).
FT TRANSMEM 277 296 Helical; (Potential).
FT TOPO_DOM 297 380 Cytoplasmic (Potential).
FT TRANSMEM 381 399 Helical; (Potential).
FT TOPO_DOM 400 410 Lumenal (Potential).
FT MOTIF 69 81 Dolichol recognition.
FT MOTIF 224 236 Dolichol recognition.
FT CARBOHYD 148 148 N-linked (GlcNAc...) (Potential).
FT VARIANT 74 74 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
//
