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Reviewed, UniProtKB/Swiss-Prot O94335 (STT3_SCHPO)

Last modified November 3, 2009. Version 51. 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

Names and origin

Protein namesRecommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
      Short name=Oligosaccharyl transferase subunit stt3
    EC=2.4.1.119
Gene names
Name: stt3
ORF Names: SPBC1271.02
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) By similarity.

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.

Subunit structure

Component of the oligosaccharyltransferase (OST) complex By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the STT3 family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid N-linked glycosylation Ref.1

Inferred from genetic interaction. Source: GeneDB_SPombe

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

oligosaccharyltransferase complex Ref.1

Inferred from genetic interaction. Source: GeneDB_SPombe

   Molecular functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
PRO_0000072292

Regions

Transmembrane20 – 4223 Potential
Transmembrane92 – 11423 Potential
Transmembrane121 – 14020 Potential
Transmembrane150 – 16920 Potential
Transmembrane176 – 19318 Potential
Transmembrane213 – 23523 Potential
Transmembrane242 – 26423 Potential
Transmembrane274 – 29623 Potential
Transmembrane308 – 33023 Potential
Transmembrane363 – 38523 Potential
Transmembrane392 – 41423 Potential

Experimental info

Sequence conflict3991S → P in BAA76479. Ref.1
Sequence conflict4611F → S in BAA76479. Ref.1
Sequence conflict739 – 75214LRRPA…IPLRV → SAVLQKLTKFL Ref.1

Sequences

Sequence LengthMass (Da)Tools
O94335-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 2ACB97DFE82B10B8

FASTA75284,974
        10         20         30         40         50         60 
MANSATITSK KGVKSHQKDW KIPLKVLILI CIAVASVSSR LFSVIRYESI IHEFDPWFNF 

        70         80         90        100        110        120 
RASKILVEQG FYNFLNWFDE RSWYPLGRVA GGTLYPGLMV TSGIIFKVLH LLRINVNIRD 

       130        140        150        160        170        180 
VCVLLAPAFS GITAIATYYL ARELKSDACG LLAAAFMGIA PGYTSRSVAG SYDNEAIAIT 

       190        200        210        220        230        240 
LLMSTFALWI KAVKSGSSFW GACTGLLYFY MVTAWGGYVF ITNMIPLHVF VLLLMGRYTS 

       250        260        270        280        290        300 
KLYIAYTTYY VIGTLASMQV PFVGFQPVST SEHMSALGVF GLLQLFAFYN YVKGLVSSKQ 

       310        320        330        340        350        360 
FQILIRFALV CLVGLATVVL FALSSTGVIA PWTGRFYSLW DTNYAKIHIP IIASVSEHQP 

       370        380        390        400        410        420 
PTWSSLFFDL QFLIWLLPVG VYLCFKELRN EHVFIIIYSV LGTYFCGVMV RLVLTLTPCV 

       430        440        450        460        470        480 
CIAAAVAIST LLDTYMGPEV EEDKVSEEAA SAKSKNKKGI FSILSFFTSG SKNIGIYSLL 

       490        500        510        520        530        540 
SRVLVISSTA YFLIMFVYHS SWVTSNAYSS PTVVLSTVLN DGSLMYIDDF REAYDWLRRN 

       550        560        570        580        590        600 
TPYDTKVMSW WDYGYQIAGM ADRITLVDNN TWNNTHIATV GKAMSSPEEK AYPILRKHDV 

       610        620        630        640        650        660 
DYILIIYGGT LGYSSDDMNK FLWMIRISQG LWPDEIVERN FFTPNGEYRT DDAATPTMRE 

       670        680        690        700        710        720 
SLLYKMSYHG AWKLFPPNQG YDRARNQKLP SKDPQLFTIE EAFTTVHHLV RLYKVKKPDT 

       730        740        750 
LGRDLKQVTL FEEGKRKKLR RPAKTNEIPL RV 

« Hide

References

« Hide 'large scale' references
[1]"Schizosaccharomyces pombe stt3+ is a functional homologue of Saccharomyces cerevisiae STT3 which regulates oligosaccharyltransferase activity."
Yoshida S., Matsuura A., Merregaert J., Anraku Y.
Yeast 15:497-505(1999) [PubMed: 10234787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.

Cross-references

Sequence databases

AB015232 Genomic DNA. Translation: BAA76479.1.
CU329671 Genomic DNA. Translation: CAA22192.1.
PIRT39338.
T43370.
RefSeqNP_595148.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO94335.

Protein family/group databases

CAZyGT66. Glycosyltransferase Family 66.

Genome annotation databases

GeneID2540190.
GenomeReviewsGene locus stt3 in contig CU329671_GR.
KEGGspo:SPBC1271.02.
NMPDRfig|4896.1.peg.1014.

Organism-specific databases

GeneDB_SpombeSPBC1271.02.

Phylogenomic databases

OMADIREENY.

Enzyme and pathway databases

BRENDA2.4.1.119. 653.

Gene expression databases

ArrayExpressO94335.

Family and domain databases

InterProIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSTT3_SCHPO
AccessionPrimary (citable) accession number: O94335
Secondary accession number(s): Q8WZK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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