Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3

Gene

stt3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic subunit of the N-oligosaccharyl transferase (OST) complex 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).By similarity

Catalytic activityi

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

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • protein N-linked glycosylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3 (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit stt3
Gene namesi
Name:stt3
ORF Names:SPBC1271.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1271.02.
PomBaseiSPBC1271.02. stt3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Topological domaini43 – 12078LumenalSequence analysisAdd
BLAST
Transmembranei121 – 14121HelicalSequence analysisAdd
BLAST
Topological domaini142 – 17534CytoplasmicSequence analysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence analysisAdd
BLAST
Topological domaini197 – 21418LumenalSequence analysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence analysisAdd
BLAST
Topological domaini236 – 2438CytoplasmicSequence analysis
Transmembranei244 – 26421HelicalSequence analysisAdd
BLAST
Topological domaini265 – 27511LumenalSequence analysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Topological domaini297 – 3037CytoplasmicSequence analysis
Transmembranei304 – 32320HelicalSequence analysisAdd
BLAST
Topological domaini324 – 36441LumenalSequence analysisAdd
BLAST
Transmembranei365 – 38521HelicalSequence analysisAdd
BLAST
Topological domaini386 – 3927CytoplasmicSequence analysis
Transmembranei393 – 41018HelicalSequence analysisAdd
BLAST
Topological domaini411 – 4111LumenalSequence analysis
Transmembranei412 – 43221HelicalSequence analysisAdd
BLAST
Topological domaini433 – 48250CytoplasmicSequence analysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence analysisAdd
BLAST
Topological domaini504 – 752249LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • oligosaccharyltransferase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3PRO_0000072292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence analysis
Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO94335.

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex.By similarity

Protein-protein interaction databases

BioGridi276723. 1 interaction.
MINTiMINT-4683335.

Family & Domainsi

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000157471.
InParanoidiO94335.
KOiK07151.
OMAiINGFDSW.
OrthoDBiEOG7QK0MM.
PhylomeDBiO94335.

Family and domain databases

InterProiIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamiPF02516. STT3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSATITSK KGVKSHQKDW KIPLKVLILI CIAVASVSSR LFSVIRYESI
60 70 80 90 100
IHEFDPWFNF RASKILVEQG FYNFLNWFDE RSWYPLGRVA GGTLYPGLMV
110 120 130 140 150
TSGIIFKVLH LLRINVNIRD VCVLLAPAFS GITAIATYYL ARELKSDACG
160 170 180 190 200
LLAAAFMGIA PGYTSRSVAG SYDNEAIAIT LLMSTFALWI KAVKSGSSFW
210 220 230 240 250
GACTGLLYFY MVTAWGGYVF ITNMIPLHVF VLLLMGRYTS KLYIAYTTYY
260 270 280 290 300
VIGTLASMQV PFVGFQPVST SEHMSALGVF GLLQLFAFYN YVKGLVSSKQ
310 320 330 340 350
FQILIRFALV CLVGLATVVL FALSSTGVIA PWTGRFYSLW DTNYAKIHIP
360 370 380 390 400
IIASVSEHQP PTWSSLFFDL QFLIWLLPVG VYLCFKELRN EHVFIIIYSV
410 420 430 440 450
LGTYFCGVMV RLVLTLTPCV CIAAAVAIST LLDTYMGPEV EEDKVSEEAA
460 470 480 490 500
SAKSKNKKGI FSILSFFTSG SKNIGIYSLL SRVLVISSTA YFLIMFVYHS
510 520 530 540 550
SWVTSNAYSS PTVVLSTVLN DGSLMYIDDF REAYDWLRRN TPYDTKVMSW
560 570 580 590 600
WDYGYQIAGM ADRITLVDNN TWNNTHIATV GKAMSSPEEK AYPILRKHDV
610 620 630 640 650
DYILIIYGGT LGYSSDDMNK FLWMIRISQG LWPDEIVERN FFTPNGEYRT
660 670 680 690 700
DDAATPTMRE SLLYKMSYHG AWKLFPPNQG YDRARNQKLP SKDPQLFTIE
710 720 730 740 750
EAFTTVHHLV RLYKVKKPDT LGRDLKQVTL FEEGKRKKLR RPAKTNEIPL

RV
Length:752
Mass (Da):84,974
Last modified:May 1, 1999 - v1
Checksum:i2ACB97DFE82B10B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991S → P in BAA76479 (PubMed:10234787).Curated
Sequence conflicti461 – 4611F → S in BAA76479 (PubMed:10234787).Curated
Sequence conflicti739 – 75214LRRPA…IPLRV → SAVLQKLTKFL in BAA76479 (PubMed:10234787).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015232 Genomic DNA. Translation: BAA76479.1.
CU329671 Genomic DNA. Translation: CAA22192.1.
PIRiT39338.
T43370.
RefSeqiNP_595148.1. NM_001021056.2.

Genome annotation databases

EnsemblFungiiSPBC1271.02.1; SPBC1271.02.1:pep; SPBC1271.02.
GeneIDi2540190.
KEGGispo:SPBC1271.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015232 Genomic DNA. Translation: BAA76479.1.
CU329671 Genomic DNA. Translation: CAA22192.1.
PIRiT39338.
T43370.
RefSeqiNP_595148.1. NM_001021056.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276723. 1 interaction.
MINTiMINT-4683335.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.

Proteomic databases

MaxQBiO94335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1271.02.1; SPBC1271.02.1:pep; SPBC1271.02.
GeneIDi2540190.
KEGGispo:SPBC1271.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC1271.02.
PomBaseiSPBC1271.02. stt3.

Phylogenomic databases

HOGENOMiHOG000157471.
InParanoidiO94335.
KOiK07151.
OMAiINGFDSW.
OrthoDBiEOG7QK0MM.
PhylomeDBiO94335.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi20801322.
PROiO94335.

Family and domain databases

InterProiIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamiPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiSTT3_SCHPO
AccessioniPrimary (citable) accession number: O94335
Secondary accession number(s): Q8WZK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.