P42864 (GPT_LEIAM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
EC=2.7.8.15

Alternative name(s):
GlcNAc-1-P transferase
Short name=G1PT
Short name=GPT
N-acetylglucosamine-1-phosphate transferase

Gene names

Name:

NAGT

Organism

Leishmania amazonensis

Taxonomic identifier

5659 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania mexicana species complex

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.
Catalytic activity	UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.
Enzyme regulation	Inhibited by tunicamycin.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	In Leishmania sp., tunicamycin-resistant variants are associated with increased levels of NAGT gene transcription due to gene amplification.
Sequence similarities	Belongs to the glycosyltransferase 4 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Inferred from electronic annotation. Source: EC phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: InterPro transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 466	466	UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase		PRO_0000108763
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Transmembrane	91 – 111	21	Helical; Potential
	Transmembrane	124 – 144	21	Helical; Potential
	Transmembrane	156 – 176	21	Helical; Potential
	Transmembrane	236 – 256	21	Helical; Potential
	Transmembrane	263 – 283	21	Helical; Potential
	Transmembrane	316 – 336	21	Helical; Potential
	Transmembrane	345 – 365	21	Helical; Potential
	Transmembrane	374 – 394	21	Helical; Potential
	Transmembrane	442 – 462	21	Helical; Potential
Amino acid modifications
	Glycosylation	59	1	N-linked (GlcNAc...) Potential
	Glycosylation	416	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P42864 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4C423662BA4072AE	FASTA	466	51,352
	10 20 30 40 50 60 MTLGLVESSR NAAFAVAAHA PVLGLILLGS IVAYVGTLRY IPNVARTLLD RNIFGIDINK 70 80 90 100 110 120 STEEQRQKFA AKRRAGQTEE KEFQKQAIPE SLGILVGAMY LSVVVVLTVC LRFLGAAGEG 130 140 150 160 170 180 LDNPYASLPG PLMTITVMLL LGFVDDVLDV KWRHKIILTA LGSLPLIMTY DGSLSVLMPC 190 200 210 220 230 240 AFGRFGLSTM NVMKEWRLGL AAPQGEPTTT FRATAPSTWF SFTVNHRSYV KVTESGAALI 250 260 270 280 290 300 YLGPVYLVYL SMLCIFCTNS INILAGVNGV EVGQSIVIAV ASVVYNLFQM RLDRQLTPDF 310 320 330 340 350 360 SSLDAAAADA RDMTSDHQLR ALLLLGPFIG VSLALWRYNR YPARVFVGDS YTYFAGTVLA 370 380 390 400 410 420 VSSITGVYSK TLLLFFAPQV FNFLISLPQL FSIVPCPRHR VPTWNPRTNL LSNSHNYTIL 430 440 450 460 NVILYLFGDM HEAKLTWAIL KCQVIACVLG FVVRYVLSAF LYDEVR

References

[1]

"The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-1-phosphate transferase gene that can be used as a dominant selectable marker in transfection." Liu X., Chang K.-P. Mol. Cell. Biol. 12:4112-4122(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MHOM/BR/73/LV78.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M96635 Genomic DNA. Translation: AAA29258.1.
PIR	A44495. S27823.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR000715. Glycosyl_transferase_4. [Graphical view]
Pfam	PF00953. Glycos_transf_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPT_LEIAM

Accession

Primary (citable) accession number: P42864

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)