Q59YV2 (ALG10_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256

Alternative name(s):
Alpha-1,2-glucosyltransferase ALG10-A
Alpha-2-glucosyltransferase ALG10
Asparagine-linked glycosylation protein 10
Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10

Gene names

Name:	ALG10
Synonyms:	DIE2
ORF Names:	CaO19.6971

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol.
Catalytic activity	Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ALG10 glucosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
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 hexosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase		PRO_0000215452
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Transmembrane	158 – 178	21	Helical; Potential
	Transmembrane	190 – 210	21	Helical; Potential
	Transmembrane	243 – 263	21	Helical; Potential
	Transmembrane	273 – 293	21	Helical; Potential
	Transmembrane	312 – 332	21	Helical; Potential
	Transmembrane	357 – 377	21	Helical; Potential
	Transmembrane	384 – 404	21	Helical; Potential
	Transmembrane	429 – 449	21	Helical; Potential
	Compositional bias	95 – 101	7	Poly-Gly
Amino acid modifications
	Glycosylation	34	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q59YV2 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 713698120987655A	FASTA	450	52,530
	10 20 30 40 50 60 MPLIIPSNDI YISIISKYVA IVIFLIFVII MFNNITHHLT QPYIDEIFHL RQCQTYCQYN 70 80 90 100 110 120 FHHWDNKITT PPGLYILGFI YSEGIKILTR SSSTGGGGGG GHLTCFNDNV LRSINLIGGV 130 140 150 160 170 180 VILPRILQQF HNGWSKNSKN QFFWSINIIS QPLLFTYYFL FYTDVSSTIL IILSLGLINY 190 200 210 220 230 240 KLLQYPMLSA LVGFMSLWFR QTNIIWIAFI ASIFIDRQIK IKTGVIDRIR QFIMKSLTNW 250 260 270 280 290 300 NKLLGYIVNI ILFVIFLKLN GGITLGDNDN HQIELHIVQV FYCFTFITFF TIPNWLNKST 310 320 330 340 350 360 IKKYYNFIIN HIILNLVIGL IIWYIMENFT IVHPFLLADN RHYAFYIYKR LLSQSYLKPL 370 380 390 400 410 420 ILMAYHFSSF QIISSLIKGG QLSFIGIFSY LIAVGLTLIP SPLFEPRYYI TPLIIFNLYI 430 440 450 NHPHNLLEFI WLNSINLITS YIFLHKGIIW

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000098 Genomic DNA. Translation: EAK95630.1.
RefSeq	XP_714677.1. XM_709584.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q59YV2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3643674.
KEGG	cal:CaO19.6971.
Organism-specific databases
CGD	CAL0000363. DIE2.
Family and domain databases
InterPro	IPR016900. Alpha1_2_glucosyltferase_Alg10. IPR007006. Glycosyltransferase_ALG10. [Graphical view]
KO	K03850.
PANTHER	PTHR12989. DIE2_ALG10. 1 hit.
Pfam	PF04922. DIE2_ALG10. 1 hit. [Graphical view]
PIRSF	PIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALG10_CANAL

Accession

Primary (citable) accession number: Q59YV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program