Q6FLZ2 (ALG1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitobiosyldiphosphodolichol beta-mannosyltransferase
EC=2.4.1.142

Alternative name(s):
Asparagine-linked glycosylation protein 1
Beta-1,4-mannosyltransferase
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase

Gene names

Name:	ALG1
Ordered Locus Names:	CAGL0K12342g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

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

General annotation (Comments)

Function	Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER By similarity.
Catalytic activity	GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase group 1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitobiosyldiphosphodolichol beta-mannosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Chitobiosyldiphosphodolichol beta-mannosyltransferase		PRO_0000080254
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	35 – 450	416	Lumenal Potential
Amino acid modifications
	Glycosylation	36	1	N-linked (GlcNAc...) Potential
	Glycosylation	201	1	N-linked (GlcNAc...) Potential
	Glycosylation	436	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6FLZ2 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 23D405BAF7FB7724	FASTA	450	51,945
	10 20 30 40 50 60 MSWIQIPWSW VVTLIVTYLS LPLIIYYLVP YIFYGNKSSK KRIIIYVLGD IGHSPRMCYH 70 80 90 100 110 120 ARSFSEKGWQ VELCGYVEEQ VPGFIAEDPN IIVHALPTLT LQGNKRSIIF LVKKVLFQVS 130 140 150 160 170 180 AIIAQLWELR GSNYMLIQNP PSIPILPIAV FYRLSGCKLI IDWHNLAYSI MQLKFNGNFY 190 200 210 220 230 240 HPVVLASYVI EYIFGKFATY NLTVTEAMKE YLVNSFGLNP KRCVVLYDRP ATQFKPLTES 250 260 270 280 290 300 ESRTKLLDSE FIRDMIPEGF NVEKGDKIIV TSTSFTPDED ISILIGALKI YDNSYENLDK 310 320 330 340 350 360 SLPKILCFVT GKGPMKERYV KDVEEHDWQH VYVKFVWLKS EDYPRLLQLC DYGVSLHKSS 370 380 390 400 410 420 SGLDLPMKIL DMYGSGIPVI AYNYPVLGEL VKYNENGLKF LDRRELHESL IFAMKDPELY 430 440 450 KKLKQGALKE SQIRWNSSWQ SAMQELKLVA

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380957 Genomic DNA. Translation: CAG61715.1.
RefSeq	XP_448752.1. XM_448752.1.
3D structure databases
ProteinModelPortal	Q6FLZ2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2889981.
GenomeReviews	Gene locus CAGL0K12342g in contig CR380957_GR.
KEGG	cgr:CAGL0K12342g.
Phylogenomic databases
eggNOG	fuNOG05192.
HOGENOM	HBG319770.
OMA	LQNPPGL.
OrthoDB	EOG4WWVT5.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. [Graphical view]
KO	K03842.
Pfam	PF00534. Glycos_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG1_CANGA

Accession

Primary (citable) accession number: Q6FLZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	July 19, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program