Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q10479 (ALG8_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
EC=2.4.1.265
Alternative name(s):
Asparagine-linked glycosylation protein 8
Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene names
Name:alg8
ORF Names:SPAC17C9.07
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + 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 = D-Glc-alpha-(1->3)-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 Ref.2.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000174167

Regions

Topological domain1 – 33Lumenal Potential
Transmembrane4 – 2421Helical; Potential
Topological domain25 – 5935Cytoplasmic Potential
Transmembrane60 – 8021Helical; Potential
Topological domain81 – 9515Lumenal Potential
Transmembrane96 – 11621Helical; Potential
Topological domain117 – 13115Cytoplasmic Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 1564Lumenal Potential
Transmembrane157 – 17721Helical; Potential
Topological domain178 – 1803Cytoplasmic Potential
Transmembrane181 – 20121Helical; Potential
Topological domain202 – 315114Lumenal Potential
Transmembrane316 – 33621Helical; Potential
Topological domain337 – 3415Cytoplasmic Potential
Transmembrane342 – 36221Helical; Potential
Topological domain363 – 38927Lumenal Potential
Transmembrane390 – 41021Helical; Potential
Topological domain411 – 4122Cytoplasmic Potential
Transmembrane413 – 43321Helical; Potential
Topological domain434 – 44310Lumenal Potential
Transmembrane444 – 46421Helical; Potential
Topological domain465 – 4739Cytoplasmic Potential
Transmembrane474 – 49421Helical; Potential
Topological domain495 – 5017Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
Q10479 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4F9A08D85390CA94

FASTA50157,606
        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

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[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.
PIRT11587.
RefSeqNP_594599.1. NM_001020027.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ10479.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC17C9.07.1; SPAC17C9.07.1:pep; SPAC17C9.07.
GeneID2542143.
GenomeReviewsGene locus alg8 in contig CU329670_GR.
KEGGspo:SPAC17C9.07.
NMPDRfig|4896.1.peg.4569.

Organism-specific databases

GeneDB_SpombeSPAC17C9.07.

Phylogenomic databases

eggNOGfuNOG05442.
GeneTreeEFGT00050000004500.
HOGENOMHBG560959.
OMAHNLNYSS.
OrthoDBEOG4J40RC.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002693-MONOMER.

Gene expression databases

ArrayExpressQ10479.

Family and domain databases

InterProIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
KOK03849.
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALG8_SCHPO
AccessionPrimary (citable) accession number: Q10479
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents