GPT_LEIAM
ID GPT_LEIAM Reviewed; 466 AA.
AC P42864;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=NAGT;
OS Leishmania amazonensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5659;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/BR/73/LV78;
RX PubMed=1324414; DOI=10.1128/mcb.12.9.4112-4122.1992;
RA Liu X., Chang K.-P.;
RT "The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania
RT amazonensis contains a functional N-acetylglucosamine-1-phosphate
RT transferase gene that can be used as a dominant selectable marker in
RT transfection.";
RL Mol. Cell. Biol. 12:4112-4122(1992).
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: Inhibited by tunicamycin.
CC {ECO:0000250|UniProtKB:Q9H3H5}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9H3H5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}.
CC -!- MISCELLANEOUS: In Leishmania sp., tunicamycin-resistant variants are
CC associated with increased levels of NAGT gene transcription due to gene
CC amplification.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
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DR EMBL; M96635; AAA29258.1; -; Genomic_DNA.
DR PIR; A44495; A44495.
DR PIR; S27823; S27823.
DR AlphaFoldDB; P42864; -.
DR SMR; P42864; -.
DR VEuPathDB; TriTrypDB:LAMA_000349000; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Membrane; Metal-binding; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..466
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108763"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 90
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 155
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 255..263
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 268
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 398..400
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 466 AA; 51352 MW; 4C423662BA4072AE CRC64;
MTLGLVESSR NAAFAVAAHA PVLGLILLGS IVAYVGTLRY IPNVARTLLD RNIFGIDINK
STEEQRQKFA AKRRAGQTEE KEFQKQAIPE SLGILVGAMY LSVVVVLTVC LRFLGAAGEG
LDNPYASLPG PLMTITVMLL LGFVDDVLDV KWRHKIILTA LGSLPLIMTY DGSLSVLMPC
AFGRFGLSTM NVMKEWRLGL AAPQGEPTTT FRATAPSTWF SFTVNHRSYV KVTESGAALI
YLGPVYLVYL SMLCIFCTNS INILAGVNGV EVGQSIVIAV ASVVYNLFQM RLDRQLTPDF
SSLDAAAADA RDMTSDHQLR ALLLLGPFIG VSLALWRYNR YPARVFVGDS YTYFAGTVLA
VSSITGVYSK TLLLFFAPQV FNFLISLPQL FSIVPCPRHR VPTWNPRTNL LSNSHNYTIL
NVILYLFGDM HEAKLTWAIL KCQVIACVLG FVVRYVLSAF LYDEVR
