Reviewed, UniProtKB/Swiss-Prot Q10479 (ALG8_SCHPO)

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:	SPAC17C9.07

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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 Ref.2.
Sequence similarities	Belongs to the ALG6/ALG8 glucosyltransferase 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 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 – 501	501	Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase		PRO_0000174167
Regions
	Topological domain	1 – 3	3	Lumenal Potential
	Transmembrane	4 – 24	21	Potential
	Topological domain	25 – 59	35	Cytoplasmic Potential
	Transmembrane	60 – 80	21	Potential
	Topological domain	81 – 95	15	Lumenal Potential
	Transmembrane	96 – 116	21	Potential
	Topological domain	117 – 131	15	Cytoplasmic Potential
	Transmembrane	132 – 152	21	Potential
	Topological domain	153 – 156	4	Lumenal Potential
	Transmembrane	157 – 177	21	Potential
	Topological domain	178 – 180	3	Cytoplasmic Potential
	Transmembrane	181 – 201	21	Potential
	Topological domain	202 – 315	114	Lumenal Potential
	Transmembrane	316 – 336	21	Potential
	Topological domain	337 – 341	5	Cytoplasmic Potential
	Transmembrane	342 – 362	21	Potential
	Topological domain	363 – 389	27	Lumenal Potential
	Transmembrane	390 – 410	21	Potential
	Topological domain	411 – 412	2	Cytoplasmic Potential
	Transmembrane	413 – 433	21	Potential
	Topological domain	434 – 443	10	Lumenal Potential
	Transmembrane	444 – 464	21	Potential
	Topological domain	465 – 473	9	Cytoplasmic Potential
	Transmembrane	474 – 494	21	Potential
	Topological domain	495 – 501	7	Lumenal Potential

Sequences

	Sequence		Length	Mass (Da)
	Q10479-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4F9A08D85390CA94	FASTA	501	57,606
	10 20 30 40 50 60 MGKLSMLYNA AIASTFVKVF LFPSYRSTDF EVHRNWLAIT HSLPISEWYK SSISEWTLDY 70 80 90 100 110 120 PPFFAYMECV LSWIAYFFGF DKAMLDPYNL NYVSPSTVVF QRGSVIVLEL VLLFALREYV 130 140 150 160 170 180 LSSNVKDQRN ALLTAIDIFL SPGLLIIDHI HFQYNGFLFG LLLWSIVLAK PEKNMLLSAA 190 200 210 220 230 240 IFSALICFKH IFLYVAPAYF VYLLRVYCFT PNFRPQFLNI LKLGSTVISI FLLAFGPWIY 250 260 270 280 290 300 MKQIPQLLSR LFPFSRGLCH AYWAPNFWAL YSFVDRVAFA VLPRFGYALN QGTSINAPTR 310 320 330 340 350 360 GLVGESSFAV LPNIPPALTF YICLGLQITV LIKLFIKPTW RVFVGAVTLC GWISFLFGWH 370 380 390 400 410 420 VHEKAILMVI LPFSILSLID RRYLEAFRPL AVSGYLSLLP LLFTLNEAPI KYLFTGAWIA 430 440 450 460 470 480 MLLTFDKCAP VPVKRVFLLN RVNIAYISGF VPLFIYNCFI HKLVMGDKFE FLPLMLLSTY 490 500 AAWGIFWSFV SLLWLYFTDL K

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA97353.1.
PIR	T11587.
RefSeq	NP_594599.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q10479.
Protein family/group databases
CAZy	GT57. Glycosyltransferase Family 57.
Genome annotation databases
GeneID	2542143.
GenomeReviews	Gene locus alg8 in contig CU329670_GR.
KEGG	spo:SPAC17C9.07.
NMPDR	fig|4896.1.peg.4569.
Organism-specific databases
GeneDB_Spombe	SPAC17C9.07.
Phylogenomic databases
eggNOG	fuNOG05442.
HOGENOM	HBG560959.
OMA	HNLNYSS.
OrthoDB	EOG93XWM0.
PhylomeDB	Q10479.
Gene expression databases
ArrayExpress	Q10479.
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_SCHPO

Accession

Primary (citable) accession number: Q10479

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)