Q05889 (LPG1_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galactofuranosyl glycosyltransferase
EC=2.4.1.-

Gene names

Name:

LPG1

Organism

Leishmania donovani

Taxonomic identifier

5661 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Glycosyltransferase that may be responsible for the addition of galactofuranosyl residues to the nascent lipophosphoglycan (LPG) chain. It could alternatively be involved in the synthesis of the galactofuranosyl donor.
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Developmental stage	Expressed throughout the life cycle with a two-fold decrease in amastigotes (LPG is 1000-fold less abundant in amastigotes than in promastigotes).
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 434	434	Galactofuranosyl glycosyltransferase		PRO_0000059105
Regions
	Topological domain	1 – 18	18	Cytoplasmic Potential
	Transmembrane	19 – 38	20	Helical; Signal-anchor for type II membrane protein
	Topological domain	39 – 434	396	Lumenal Potential
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	100	1	N-linked (GlcNAc...) Potential
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	388	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q05889 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: BBE33A0EAE5079B8	FASTA	434	51,016
	10 20 30 40 50 60 MAPPRWHHDR RRMAIFVRVG LYTLLFLMGY VVPLIIFYNR SRADTFEDTP RSGEAFISDE 70 80 90 100 110 120 NFFHCIAERL SYKEQHPARI PYVLIPVTMD YQDIKQLFCN ITVPMTYIMF INNGMFRPLR 130 140 150 160 170 180 SLLDRLAVDL RDYVDQNLFI IHHPENIAYA SAVNEGLRHA LNFSVAKVPW VFITNADVRF 190 200 210 220 230 240 APGLIDEFVS QANEKTQGQL ERIRRLDQEI IAEARTLRNV PNRRFAFRSS QHPIITASSL 250 260 270 280 290 300 PYRIRTMPPE EMKKQFADTY GIFYTDHKDF MATFALSRLA IATVGFFDEN YYPAYGEDHD 310 320 330 340 350 360 YVWRMAALGY QKYFSEPGKF VHFENANLNV GGSARNRGIF KNTAYFLQSV KFGRMNYQPF 370 380 390 400 410 420 RLQYRRAKWF PDGVTIYQDT GRNPLPFNGT IPLDMWVLDT DRRRSIWEIG ENIRCHRDYK 430 PYSMKLLDFP VDPS

References

[1]

"Isolation of virulence genes directing surface glycosyl-phosphatidylinositol synthesis by functional complementation of Leishmania." Ryan K.A., Garraway L.A., Descoteaux A., Turco S.J., Beverley S.M. Proc. Natl. Acad. Sci. U.S.A. 90:8609-8613(1993) [PubMed: 8378337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Ld4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11348 Unassigned DNA. Translation: AAA03083.1.
3D structure databases
ProteinModelPortal	Q05889.
ModBase	Search...
Protein family/group databases
CAZy	GT40. Glycosyltransferase Family 40.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPG1_LEIDO

Accession

Primary (citable) accession number: Q05889

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 28, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)