GPT_HUMAN
ID GPT_HUMAN Reviewed; 408 AA.
AC Q9H3H5; O15216; Q86WV9; Q9BWE6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE EC=2.7.8.15 {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443, ECO:0000269|PubMed:9451016};
DE AltName: Full=GlcNAc-1-P transferase {ECO:0000303|PubMed:29459785};
DE Short=G1PT;
DE Short=GPT {ECO:0000303|PubMed:29459785};
DE AltName: Full=N-acetylglucosamine-1-phosphate transferase;
GN Name=DPAGT1 {ECO:0000303|PubMed:12872255, ECO:0000303|PubMed:22742743,
GN ECO:0000303|PubMed:29459785, ECO:0000312|HGNC:HGNC:2995}; Synonyms=DPAGT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND PATHWAY.
RC TISSUE=Lung;
RX PubMed=9451016; DOI=10.1093/glycob/8.1.77;
RA Eckert V., Blank M., Mazhari-Tabrizi R., Mumberg D., Funk M., Schwarz R.T.;
RT "Cloning and functional expression of the human GlcNAc-1-P transferase, the
RT enzyme for the committed step of the dolichol cycle, by heterologous
RT complementation in Saccharomyces cerevisiae.";
RL Glycobiology 8:77-85(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Dagnino F., Regis S., Filocamo M., Gatti R.;
RT "Putative genomic sequence of GlcNAc-1-P transferase on chromosome 11q23.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TUNICAMYCIN
RP INHIBITOR, FUNCTION, SUBUNIT, PATHWAY, TOPOLOGY, ACTIVITY REGULATION,
RP COFACTOR, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-252.
RX PubMed=29459785; DOI=10.1038/s41594-018-0031-y;
RA Yoo J., Mashalidis E.H., Kuk A.C.Y., Yamamoto K., Kaeser B., Ichikawa S.,
RA Lee S.Y.;
RT "GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for
RT inhibition of N-glycosylation.";
RL Nat. Struct. Mol. Biol. 25:217-224(2018).
RN [5] {ECO:0007744|PDB:5LEV, ECO:0007744|PDB:5O5E, ECO:0007744|PDB:6FM9, ECO:0007744|PDB:6FWZ}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF WILD-TYPE AND VARIANT CMS13
RP GLY-264 IN COMPLEXES WITH UDP-N-ACETYLGLUCOSAMINE AND TUNICAMYCIN,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP PATHWAY, ACTIVITY REGULATION, SUBUNIT, TOPOLOGY, CHARACTERIZATION OF
RP VARIANT CDG1J CYS-170, CHARACTERIZATION OF VARIANTS CMS13 ILE-108; MET-120;
RP SER-160; LEU-168; ILE-171; SER-192 AND GLY-264, AND MUTAGENESIS OF PRO-30;
RP ILE-69; ALA-114; ASP-115; ASP-116; TRP-122; LYS-125; LEU-168; ASN-182;
RP ASN-185; ASP-252; VAL-264; ARG-301; HIS-302 AND ARG-303.
RX PubMed=30388443; DOI=10.1016/j.cell.2018.10.037;
RA Dong Y.Y., Wang H., Pike A.C.W., Cochrane S.A., Hamedzadeh S.,
RA Wyszynski F.J., Bushell S.R., Royer S.F., Widdick D.A., Sajid A.,
RA Boshoff H.I., Park Y., Lucas R., Liu W.M., Lee S.S., Machida T., Minall L.,
RA Mehmood S., Belaya K., Liu W.W., Chu A., Shrestha L., Mukhopadhyay S.M.M.,
RA Strain-Damerell C., Chalk R., Burgess-Brown N.A., Bibb M.J.,
RA Barry Iii C.E., Robinson C.V., Beeson D., Davis B.G., Carpenter E.P.;
RT "Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance
RT TB Antibiotic Design.";
RL Cell 175:1045-1058(2018).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP VAL-393.
RC TISSUE=Lung;
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 [7]
RP VARIANT CDG1J CYS-170.
RX PubMed=12872255; DOI=10.1002/humu.10239;
RA Wu X., Rush J.S., Karaoglu D., Krasnewich D., Lubinsky M.S., Waechter C.J.,
RA Gilmore R., Freeze H.H.;
RT "Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1
RT phosphate transferase (DPAGT1) causes a novel congenital disorder of
RT glycosylation type Ij.";
RL Hum. Mutat. 22:144-150(2003).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-9.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [9]
RP VARIANTS CMS13 ILE-108; ILE-117; MET-120; SER-160; SER-192 AND GLY-264.
RX PubMed=22742743; DOI=10.1016/j.ajhg.2012.05.022;
RA Belaya K., Finlayson S., Slater C.R., Cossins J., Liu W.W., Maxwell S.,
RA McGowan S.J., Maslau S., Twigg S.R., Walls T.J., Pascual Pascual S.I.,
RA Palace J., Beeson D.;
RT "Mutations in DPAGT1 cause a limb-girdle congenital myasthenic syndrome
RT with tubular aggregates.";
RL Am. J. Hum. Genet. 91:193-201(2012).
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:29459785, ECO:0000269|PubMed:30388443,
CC ECO:0000269|PubMed:9451016}.
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:29459785, ECO:0000269|PubMed:30388443,
CC ECO:0000269|PubMed:9451016};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443};
CC -!- ACTIVITY REGULATION: Activated by mannosylphosphoryldolichol and
CC phospholipids such as phosphatidylglycerol and phosphatidylcholine
CC (Probable). Inhibited by natural nucleoside antibiotic tunicamycin,
CC which acts as a structural analog and competitor of UDP-GlcNAc
CC (PubMed:9451016, PubMed:29459785, PubMed:30388443).
CC {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443,
CC ECO:0000269|PubMed:9451016, ECO:0000305|PubMed:29459785}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 uM for UDP-N-acetylglucosamine {ECO:0000269|PubMed:30388443};
CC KM=36 uM for dolichol phosphate {ECO:0000269|PubMed:30388443};
CC Note=kcat is 0.21 min(-1) with UDP-N-acetylglucosamine. kcat is 0.20
CC min(-1) with dolichol phosphate. {ECO:0000269|PubMed:30388443};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443,
CC ECO:0000269|PubMed:9451016}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29459785,
CC ECO:0000269|PubMed:30388443}.
CC -!- INTERACTION:
CC Q9H3H5; P42858: HTT; NbExp=3; IntAct=EBI-3922860, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein {ECO:0000269|PubMed:29459785,
CC ECO:0000269|PubMed:30388443}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H3H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3H5-2; Sequence=VSP_001803;
CC Name=3;
CC IsoId=Q9H3H5-3; Sequence=VSP_008886;
CC -!- DISEASE: Congenital disorder of glycosylation 1J (CDG1J) [MIM:608093]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:12872255,
CC ECO:0000269|PubMed:30388443}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 13 (CMS13) [MIM:614750]: A
CC form of congenital myasthenic syndrome, a group of disorders
CC characterized by failure of neuromuscular transmission, including pre-
CC synaptic, synaptic, and post-synaptic disorders that are not of
CC autoimmune origin. Clinical features are easy fatigability and muscle
CC weakness. CMS13 is characterized by muscle weakness mostly affecting
CC proximal limb muscles, minimal involvement of facial, ocular and bulbar
CC muscles, and tubular aggregates present on muscle biopsy. Symptoms
CC include difficulty walking and frequent falls. Younger patients show
CC hypotonia and poor head control. Neurophysiological features indicate a
CC disorder of neuromuscular transmission on electromyography.
CC {ECO:0000269|PubMed:22742743, ECO:0000269|PubMed:30388443}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-N-
CC acetylglucosamine--dolichyl-phosphate N-
CC acetylglucosaminephosphotransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_543";
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DR EMBL; Z82022; CAB04787.1; -; mRNA.
DR EMBL; AF070443; AAG43168.1; -; Genomic_DNA.
DR EMBL; AF069061; AAG43168.1; JOINED; Genomic_DNA.
DR EMBL; BT006802; AAP35448.1; -; mRNA.
DR EMBL; BC000325; AAH00325.1; -; mRNA.
DR EMBL; BC047771; AAH47771.1; -; mRNA.
DR CCDS; CCDS8411.1; -. [Q9H3H5-1]
DR RefSeq; NP_001373.2; NM_001382.3. [Q9H3H5-1]
DR RefSeq; XP_016872782.1; XM_017017293.1. [Q9H3H5-3]
DR PDB; 5LEV; X-ray; 3.20 A; A=1-408.
DR PDB; 5O5E; X-ray; 3.40 A; A=1-408.
DR PDB; 6BW5; X-ray; 3.10 A; A/B/C/D=1-408.
DR PDB; 6BW6; X-ray; 2.95 A; A/B/C/D=1-408.
DR PDB; 6FM9; X-ray; 3.60 A; A=1-408.
DR PDB; 6FWZ; X-ray; 3.10 A; A=1-408.
DR PDB; 6JQ3; X-ray; 2.50 A; P=204-211.
DR PDBsum; 5LEV; -.
DR PDBsum; 5O5E; -.
DR PDBsum; 6BW5; -.
DR PDBsum; 6BW6; -.
DR PDBsum; 6FM9; -.
DR PDBsum; 6FWZ; -.
DR PDBsum; 6JQ3; -.
DR AlphaFoldDB; Q9H3H5; -.
DR SMR; Q9H3H5; -.
DR BioGRID; 108133; 14.
DR IntAct; Q9H3H5; 12.
DR STRING; 9606.ENSP00000386597; -.
DR BindingDB; Q9H3H5; -.
DR ChEMBL; CHEMBL4739704; -.
DR GlyGen; Q9H3H5; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H3H5; -.
DR PhosphoSitePlus; Q9H3H5; -.
DR BioMuta; DPAGT1; -.
DR DMDM; 18202943; -.
DR EPD; Q9H3H5; -.
DR jPOST; Q9H3H5; -.
DR MassIVE; Q9H3H5; -.
DR MaxQB; Q9H3H5; -.
DR PaxDb; Q9H3H5; -.
DR PeptideAtlas; Q9H3H5; -.
DR PRIDE; Q9H3H5; -.
DR ProteomicsDB; 80717; -. [Q9H3H5-1]
DR ProteomicsDB; 80718; -. [Q9H3H5-2]
DR ProteomicsDB; 80719; -. [Q9H3H5-3]
DR Antibodypedia; 32608; 158 antibodies from 23 providers.
DR DNASU; 1798; -.
DR Ensembl; ENST00000354202.9; ENSP00000346142.4; ENSG00000172269.20. [Q9H3H5-1]
DR Ensembl; ENST00000409993.6; ENSP00000386597.2; ENSG00000172269.20. [Q9H3H5-1]
DR GeneID; 1798; -.
DR KEGG; hsa:1798; -.
DR MANE-Select; ENST00000354202.9; ENSP00000346142.4; NM_001382.4; NP_001373.2.
DR UCSC; uc001pvi.4; human. [Q9H3H5-1]
DR CTD; 1798; -.
DR DisGeNET; 1798; -.
DR GeneCards; DPAGT1; -.
DR GeneReviews; DPAGT1; -.
DR HGNC; HGNC:2995; DPAGT1.
DR HPA; ENSG00000172269; Low tissue specificity.
DR MalaCards; DPAGT1; -.
DR MIM; 191350; gene.
DR MIM; 608093; phenotype.
DR MIM; 614750; phenotype.
DR neXtProt; NX_Q9H3H5; -.
DR OpenTargets; ENSG00000172269; -.
DR Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect.
DR Orphanet; 86309; DPAGT1-CDG.
DR PharmGKB; PA27460; -.
DR VEuPathDB; HostDB:ENSG00000172269; -.
DR eggNOG; KOG2788; Eukaryota.
DR GeneTree; ENSGT00390000011424; -.
DR HOGENOM; CLU_029942_0_1_1; -.
DR InParanoid; Q9H3H5; -.
DR OMA; LVWMGPM; -.
DR OrthoDB; 1079130at2759; -.
DR PhylomeDB; Q9H3H5; -.
DR TreeFam; TF313734; -.
DR BRENDA; 2.7.8.15; 2681.
DR PathwayCommons; Q9H3H5; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR Reactome; R-HSA-4549356; Defective DPAGT1 causes CDG-1j, CMSTA2.
DR SignaLink; Q9H3H5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 1798; 607 hits in 1089 CRISPR screens.
DR ChiTaRS; DPAGT1; human.
DR GeneWiki; DPAGT1; -.
DR GenomeRNAi; 1798; -.
DR Pharos; Q9H3H5; Tbio.
DR PRO; PR:Q9H3H5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H3H5; protein.
DR Bgee; ENSG00000172269; Expressed in mucosa of transverse colon and 186 other tissues.
DR ExpressionAtlas; Q9H3H5; baseline and differential.
DR Genevisible; Q9H3H5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IDA:MGI.
DR GO; GO:0019348; P:dolichol metabolic process; IEA:Ensembl.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:Ensembl.
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; Alternative splicing; Congenital disorder of glycosylation;
KW Congenital myasthenic syndrome; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Glycosyltransferase; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108761"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 11..38
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 39..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 59..78
FT /note="Helical; Name=Helix 2"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 79..91
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 92..118
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 119..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 122..143
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 144..166
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 167..186
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 187..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 193..213
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 214..218
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 219..242
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 243..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 251..269
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 270..271
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 272..293
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 294..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TRANSMEM 376..400
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000269|PubMed:29459785"
FT TOPO_DOM 401..408
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29459785"
FT BINDING 44..46
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30388443"
FT BINDING 46
FT /ligand="tunicamycin A1"
FT /ligand_id="ChEBI:CHEBI:64245"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6"
FT BINDING 56
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30388443"
FT BINDING 119
FT /ligand="tunicamycin A1"
FT /ligand_id="ChEBI:CHEBI:64245"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0007744|PDB:6BW5"
FT BINDING 125
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000305|PubMed:30388443"
FT BINDING 178..186
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000305|PubMed:30388443"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30388443,
FT ECO:0007744|PDB:6FWZ"
FT BINDING 185
FT /ligand="tunicamycin A1"
FT /ligand_id="ChEBI:CHEBI:64245"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0007744|PDB:6BW6"
FT BINDING 191
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30388443"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30388443,
FT ECO:0007744|PDB:6FWZ"
FT BINDING 252
FT /ligand="tunicamycin A1"
FT /ligand_id="ChEBI:CHEBI:64245"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0007744|PDB:6BW5"
FT BINDING 301..303
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30388443"
FT BINDING 303
FT /ligand="tunicamycin A1"
FT /ligand_id="ChEBI:CHEBI:64245"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008886"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9451016"
FT /id="VSP_001803"
FT VARIANT 9
FT /note="M -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036422"
FT VARIANT 108
FT /note="M -> I (in CMS13; strongly reduced enzyme activity;
FT dbSNP:rs376039938)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068810"
FT VARIANT 117
FT /note="V -> I (in CMS13; mildly reduced enzyme activity;
FT dbSNP:rs387907243)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068811"
FT VARIANT 120
FT /note="L -> M (in CMS13; strongly reduced enzyme activity;
FT dbSNP:rs387907244)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068812"
FT VARIANT 160
FT /note="G -> S (in CMS13; increased enzyme activity;
FT dbSNP:rs762676399)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068813"
FT VARIANT 170
FT /note="Y -> C (in CDG1J; strongly reduced enzyme activity;
FT dbSNP:rs28934876)"
FT /evidence="ECO:0000269|PubMed:12872255,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_017243"
FT VARIANT 192
FT /note="G -> S (in CMS13; strongly reduced enzyme activity;
FT dbSNP:rs768464558)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068814"
FT VARIANT 264
FT /note="V -> G (in CMS13; increased enzyme activity;
FT dbSNP:rs387907245)"
FT /evidence="ECO:0000269|PubMed:22742743,
FT ECO:0000269|PubMed:30388443"
FT /id="VAR_068815"
FT VARIANT 393
FT /note="I -> V (in dbSNP:rs643788)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_011391"
FT MUTAGEN 30
FT /note="P->S: Mildly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 69
FT /note="I->N: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 103
FT /note="L->F: Impairs protein stability."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 114
FT /note="A->G: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 115
FT /note="D->A,N: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 115
FT /note="D->E: Mildly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 116
FT /note="D->A,N: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 122
FT /note="W->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 125
FT /note="K->A,E,N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 168
FT /note="L->P: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 182
FT /note="N->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 185
FT /note="N->A,D: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 252
FT /note="D->A: Reduces binding to inhibitor. Nearly abolishes
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:29459785,
FT ECO:0000269|PubMed:30388443"
FT MUTAGEN 264
FT /note="V->M: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 301
FT /note="R->C,H: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 302
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 303
FT /note="R->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT MUTAGEN 385
FT /note="L->R: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:30388443"
FT CONFLICT 33
FT /note="R -> L (in Ref. 1; CAB04787)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="P -> H (in Ref. 2; AAG43168)"
FT /evidence="ECO:0000305"
FT HELIX 9..31
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 92..118
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:6BW6"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:5O5E"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 193..213
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 219..242
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 251..269
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6BW6"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6BW6"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:6BW6"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6BW5"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:6BW6"
FT HELIX 376..398
FT /evidence="ECO:0007829|PDB:6BW6"
SQ SEQUENCE 408 AA; 46090 MW; 0AE10EFE55E7B9E0 CRC64;
MWAFSELPMP LLINLIVSLL GFVATVTLIP AFRGHFIAAR LCGQDLNKTS RQQIPESQGV
ISGAVFLIIL FCFIPFPFLN CFVKEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRPILG LHLDLGILYY VYMGLLAVFC
TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDCRDD HVFSLYFMIP FFFTTLGLLY
HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP
RHRIPRLNIK TGKLEMSYSK FKTKSLSFLG TFILKVAESL QLVTVHQSET EDGEFTECNN
MTLINLLLKV LGPIHERNLT LLLLLLQILG SAITFSIRYQ LVRLFYDV
