Reviewed, UniProtKB/Swiss-Prot Q2U6A4 (ALG3_ASPOR)

Names and origin

Protein names

Recommended name:
    Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
    EC=2.4.1.130
Alternative name(s):
    Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
    Asparagine-linked glycosylation protein 6

Gene names

Name:	alg3
ORF Names:	AO090120000319

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol By similarity.
Catalytic activity	Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the ALG3 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dolichyl-phosphate-mannose-glycolipid alpha-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 – 413	413	Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase		PRO_0000350923
Regions
	Topological domain	1 – 18	18	Lumenal Potential
	Transmembrane	19 – 39	21	Potential
	Topological domain	40 – 95	56	Cytoplasmic Potential
	Transmembrane	96 – 116	21	Potential
	Topological domain	117 – 139	23	Lumenal Potential
	Transmembrane	140 – 160	21	Potential
	Topological domain	161 – 181	21	Cytoplasmic Potential
	Transmembrane	182 – 202	21	Potential
	Topological domain	203 – 207	5	Lumenal Potential
	Transmembrane	208 – 228	21	Potential
	Topological domain	229 – 261	33	Cytoplasmic Potential
	Transmembrane	262 – 282	21	Potential
	Topological domain	283 – 304	22	Lumenal Potential
	Transmembrane	305 – 325	21	Potential
	Topological domain	326 – 372	47	Cytoplasmic Potential
	Transmembrane	373 – 393	21	Potential
	Topological domain	394 – 413	20	Lumenal Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2U6A4-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: D73845A54C5E4F76	FASTA	413	46,649
	10 20 30 40 50 60 MELKHFIHEL CLNPRHTKWI APLLVIGDAF LCALIIWKIP YTEIDWTTYM QQIALYISGE 70 80 90 100 110 120 RDYTLIKGST GPLVYPAAHV YSYMALYHLT DEGRDILFGQ ILFAVLYLVT LAVVMVCYRQ 130 140 150 160 170 180 SGAPPYLFPL LVLSKRLHSV FVLRLFNDGL AVCAMWIAIL LFQNKKWTAG VTAWTVGVGI 190 200 210 220 230 240 KMTLLLLAPA IAVVTVLSLS LVPSIRLGIL ALLIQVLLAI PFLQGNPIGY VARAFELTRQ 250 260 270 280 290 300 FMFKWTVNWR FVGEDLFLSK QFSLALLGLH IFLLGLFVTT GWLRPSGSNV PDFLRSLLQG 310 320 330 340 350 360 RQRTVVLSKS FIMTVMLTSL AIGLLCARSL HYQFFAYLSW ATPCLLWRAR LHPILIYAIW 370 380 390 400 410 ALQEWAWNVY PSTNASSSVV VFSLAVQVFG VLLNSRNALS DAPPRRKGKE HIQ

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007166 Genomic DNA. Translation: BAE62911.1.
RefSeq	XP_001824044.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5996303.
GenomeReviews	Gene locus alg3 in contig AP007166_GR.
KEGG	aor:AO090120000319.
Phylogenomic databases
OrthoDB	EOG9T4FBS.
PhylomeDB	Q2U6A4.
Family and domain databases
InterPro	IPR007873. Glycosyltransferase_ALG3. [Graphical view]
PANTHER	PTHR12646. ALG3. 1 hit.
Pfam	PF05208. ALG3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG3_ASPOR

Accession

Primary (citable) accession number: Q2U6A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	January 24, 2006
Last modified:	January 19, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)