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Reviewed, UniProtKB/Swiss-Prot Q10176 (OST1_SCHPO)

Last modified January 19, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
    EC=2.4.1.119
Alternative name(s):
    Oligosaccharyl transferase subunit alpha
Gene names
Name: ost1
ORF Names: SPAC27F1.07
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.

Catalytic activity

Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the OST1 family.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
Transmembrane
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid glycosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentendoplasmic reticulum

Inferred from direct assay. Source: GeneDB_SPombe

external side of plasma membrane

Traceable author statement. Source: GeneDB_SPombe

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 450432Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
PRO_0000021959

Regions

Topological domain19 – 424406Lumenal Potential
Transmembrane425 – 44420 Potential
Topological domain445 – 4506Cytoplasmic Potential

Amino acid modifications

Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q10176-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8C96E34C2EEE1F11

FASTA45051,684
        10         20         30         40         50         60 
MLVLKLLLWS IISGLSLAEQ VWRNSNAIRT IDLRSTYTKT LTSLIIVNEG DEPQNTYRYF 

        70         80         90        100        110        120 
QQTSPGESVL SLSVSIKEEE KKGTNPIKVN NNVYDIPLQP PVKPGESRTL LIQAGLDGGV 

       130        140        150        160        170        180 
RPLPAAVDQD EEQYLVYLTT LYLDSPYTTD LQRTRLILPS AKIDTYTTYN IDGAELPNRV 

       190        200        210        220        230        240 
GNTLVYESRE TITGEDNDLG EIYVRYEHTV PIPRGADLYV QIDMHEYRKM LEVSERVVFE 

       250        260        270        280        290        300 
NHAAKLKSNF DRAKWYMGNF YNPVSTAINR VVYSLPRNSK DVYYTDEVGN ITTSHMRVEP 

       310        320        330        340        350        360 
HQTWIELNPR YPVFGGWNYL FQLDWKMPYE EFRSSKNRRE YLDIPLAWSP GDMIYEKAVW 

       370        380        390        400        410        420 
SYVFPEGATN IEIEMPVEIS NSNVTKIHKF LDTLGRQVFT YEALNVTDGV PSDIVHISYE 

       430        440        450 
YNSSAFFLRI AIITTLLILL AAAAYMIWAP

« Hide

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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: ATCC 38366 / 972.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAA93296.1.
PIRT38465.
RefSeqNP_594536.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ10176.

Genome annotation databases

GeneID2541636.
GenomeReviewsGene locus ost1 in contig CU329670_GR.
KEGGspo:SPAC27F1.07.
NMPDRfig|4896.1.peg.4506.

Organism-specific databases

GeneDB_SpombeSPAC27F1.07.

Phylogenomic databases

eggNOGfuNOG05907.
OMAFLNITFG.
OrthoDBEOG9FBK99.
PhylomeDBQ10176.

Enzyme and pathway databases

BRENDA2.4.1.119. 653.

Gene expression databases

ArrayExpressQ10176.

Family and domain databases

InterProIPR007676. Ribophorin_I.
[Graphical view]
PANTHERPTHR21049. Ribophorin_I. 1 hit.
PfamPF04597. Ribophorin_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameOST1_SCHPO
AccessionPrimary (citable) accession number: Q10176
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 19, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents