Reviewed, UniProtKB/Swiss-Prot Q5AJD2 (ALG8_CANAL)

Names and origin

Protein names

Recommended name:
    Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase
    Asparagine-linked glycosylation protein 8

Gene names

Name:	ALG8
ORF Names:	CaO19.1659, CaO19.9228

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Adds the second 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 Glc1Man9GlcNAc(2)-PP-Dol By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the ALG6/ALG8 glucosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 587	587	Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase		PRO_0000278328
Regions
	Topological domain	1 – 41	41	Lumenal Potential
	Transmembrane	42 – 62	21	Potential
	Topological domain	63 – 139	77	Cytoplasmic Potential
	Transmembrane	140 – 160	21	Potential
	Topological domain	161 – 169	9	Lumenal Potential
	Transmembrane	170 – 192	23	Potential
	Topological domain	193 – 220	28	Cytoplasmic Potential
	Transmembrane	221 – 241	21	Potential
	Topological domain	242 – 274	33	Lumenal Potential
	Transmembrane	275 – 295	21	Potential
	Topological domain	296 – 298	3	Cytoplasmic Potential
	Transmembrane	299 – 321	23	Potential
	Topological domain	322 – 378	57	Lumenal Potential
	Transmembrane	379 – 399	21	Potential
	Topological domain	400 – 415	16	Cytoplasmic Potential
	Transmembrane	416 – 436	21	Potential
	Topological domain	437 – 443	7	Lumenal Potential
	Transmembrane	444 – 464	21	Potential
	Topological domain	465 – 466	2	Cytoplasmic Potential
	Transmembrane	467 – 487	21	Potential
	Topological domain	488 – 518	31	Lumenal Potential
	Transmembrane	519 – 539	21	Potential
	Topological domain	540 – 557	18	Cytoplasmic Potential
	Transmembrane	558 – 578	21	Potential
	Topological domain	579 – 587	9	Lumenal Potential
	Compositional bias	24 – 39	16	Thr-rich

Sequences

	Sequence		Length	Mass (Da)
	Q5AJD2-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 27BF61F4B8F67FEA	FASTA	587	67,887
	10 20 30 40 50 60 MAKKKSTGPQ PSLSSSPNGR AKVTAETITT TTTTTTDTTN SYSLLNIWVI SLALKILLFI 70 80 90 100 110 120 GYHSTDFDVH RNWLAITNKL PISQWYIENT SQWTLDYPPF FAYFEYLLSL LVPRFVANDG 130 140 150 160 170 180 CLDIVEIGQY GLPTIYFQRL TVIISELVLF YALQTIVKTS PTLSAKRRMY VATASLALSP 190 200 210 220 230 240 GLILIDHIHF QYNGMMYGIL LLCINSARLQ QYLLCGFWFS VLLCFKHIYL YLAPAVFIFL 250 260 270 280 290 300 LRGYCLKFNW NKRKNFFINI FNFIQWINLF KLGSIVILVF IIAFGPFYNV LPQLISRLFP 310 320 330 340 350 360 FSRGLTHAYW APNIWAVYSF LDRILIQIYK KIPMSKYPLL KIFQFDPNSL NNDQLLKTST 370 380 390 400 410 420 RGIVGDIEFF ILPNITPKLT FLLTLFYQIM ALIPLFIQPT YRRFVGALTL CGYASFLFGW 430 440 450 460 470 480 HVHEKAILLV IFPMTLLVAR DQKLLTPFNL LVSCGYGSLF PLIFTCNEWL IKVVYTYTWY 490 500 510 520 530 540 IIFYFNFRKV VRPSKNNIIG NGIGNGNGKG GGIILDRMVN LYILLFNVVV IITSLFDLFK 550 560 570 580 HKYPVLQNFE FLNLMIYSVY CAIGIISSWN GFCWLYFIDD GIWNQDQ

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACQ01000014 Genomic DNA. Translation: EAL02821.1. AACQ01000013 Genomic DNA. Translation: EAL02948.1.
RefSeq	XP_721617.1. XP_721736.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3636562. 3636691.
KEGG	cal:CaO19.1659. cal:CaO19.9228.
Organism-specific databases
CGD	CAL0000044. ALG8.
Phylogenomic databases
OMA	ARERRYV.
OrthoDB	EOG93XWM0.
Family and domain databases
InterPro	IPR004856. Glycosyltransferase_ALG6/ALG8. [Graphical view]
PANTHER	PTHR12413. Alg6_Alg8. 1 hit.
Pfam	PF03155. Alg6_Alg8. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG8_CANAL

Accession

Primary (citable) accession number: Q5AJD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	April 26, 2005
Last modified:	November 24, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)