Q09226 (ALG6_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
EC=2.4.1.267

Alternative name(s):
Asparagine-linked glycosylation protein 6 homolog
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase

Gene names

ORF Names:

C08B11.8

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Adds the first 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 Man9GlcNAc(2)-PP-Dol By similarity.
Catalytic activity	Dolichyl beta-D-glucosyl phosphate + 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->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 Potential.
Sequence similarities	Belongs to the ALG6/ALG8 glucosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
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 – 503	503	Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase		PRO_0000174157
Regions
	Transmembrane	47 – 67	21	Helical; Potential
	Transmembrane	152 – 172	21	Helical; Potential
	Transmembrane	182 – 202	21	Helical; Potential
	Transmembrane	212 – 232	21	Helical; Potential
	Transmembrane	233 – 253	21	Helical; Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Transmembrane	333 – 353	21	Helical; Potential
	Transmembrane	383 – 403	21	Helical; Potential
	Transmembrane	421 – 441	21	Helical; Potential
	Transmembrane	444 – 464	21	Helical; Potential
	Transmembrane	475 – 495	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q09226 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 06A5F20DE1AEFC65	FASTA	503	57,907
	10 20 30 40 50 60 MKERIKDKAW RPQFIKLNNP DTSKKIVSQK SKKPEIVDLS SPGNNDLVTI SILCVLLCFQ 70 80 90 100 110 120 LAISLNPHSG ESQPPMYGDY EAQRHWMEIT VNLPIEQWYL NGTHNDLLYW GLDYPPITAY 130 140 150 160 170 180 HHYLLGVISN KINKKWVELT TSRGYESIAH KLFMRLSAII PFYIFYLPPL IFYFTRSKKM 190 200 210 220 230 240 SPILYALALL YPSLLVIDNG HFQYNSISLG LFLATYMFLT KNFTIIGSIL FVAALNYKQM 250 260 270 280 290 300 ELYHALPVFV FILARSINKT QLFNSFRRIL TIGLFVVGTF LIIWLPFLLT GTAKDVIIRV 310 320 330 340 350 360 FPFNRGLYED KVASFWCAFS FILKRLPLQS VQIYISTALV LAGSAPSLLV LFLRPTEKQF 370 380 390 400 410 420 RISLTATGLS FFLFSFHVHE KTILLAAVPA LLLISEYTSL VIWFLNITNI SIFSLCVKDN 430 440 450 460 470 480 FALSLSFFFA YFVVSYAYTA PRKISHILTI LIGFAICILE LYGPSNQRFP HIYQLANAFF 490 500 SCVHFIYFLL YLSFASFEKT KKE

References

[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46676 Genomic DNA. Translation: CAA86666.1.
PIR	T19071.
RefSeq	NP_495685.1. NM_063284.1.
UniGene	Cel.15950.
3D structure databases
ProteinModelPortal	Q09226.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09226.
Protein family/group databases
CAZy	GT57. Glycosyltransferase Family 57.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C08B11.8; C08B11.8; C08B11.8.
GeneID	182392.
KEGG	cel:C08B11.8.
NMPDR	fig|6239.3.peg.6445.
UCSC	C08B11.8. c. elegans.
Organism-specific databases
CTD	182392.
WormBase	C08B11.8; CE01478; WBGene00007435.
Phylogenomic databases
eggNOG	meNOG04127.
GeneTree	EMGT00050000012559.
HOGENOM	HBG621987.
InParanoid	Q09226.
OMA	FLISVIT.
PhylomeDB	Q09226.
Gene expression databases
ArrayExpress	Q09226.
Family and domain databases
InterPro	IPR004856. Glyco_trans_ALG6/ALG8. [Graphical view]
KO	K03848.
PANTHER	PTHR12413. Alg6_Alg8. 1 hit.
Pfam	PF03155. Alg6_Alg8. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	917396.

Entry information

Entry name

ALG6_CAEEL

Accession

Primary (citable) accession number: Q09226

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project