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Q3TDQ1 (STT3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Short name=Oligosaccharyl transferase subunit STT3B
Short name=STT3-B
EC=2.4.1.119
Alternative name(s):
B6dom1 antigen
Source of immunodominant MHC-associated peptides
Gene names
Name:Stt3b
Synonyms:Simp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor 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). SST3B seems to be involved in complex substrate specificity 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.

Subunit structure

Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Polymorphism

In strains 129, C57BL/10, C57BL/6 and LP Glu-776 correlates with a B6dom1-positive phenotype, Asp-776 is found in resistant strains. The B6dom1 minor histocompatibilty antigen (MiHA) is used as a model antigen in studying immunodominance.

Sequence caution

The sequence AAH13054.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 823822Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
PRO_0000246002

Regions

Transmembrane62 – 8221Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane166 – 18621Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane240 – 25617Helical; Potential
Transmembrane260 – 28021Helical; Potential
Transmembrane289 – 30921Helical; Potential
Transmembrane317 – 33721Helical; Potential
Transmembrane348 – 36821Helical; Potential
Transmembrane408 – 42821Helical; Potential
Transmembrane438 – 45821Helical; Potential
Transmembrane461 – 48121Helical; Potential
Transmembrane535 – 55521Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue181Phosphoserine By similarity
Modified residue291Phosphoserine By similarity
Modified residue4951Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
Modified residue4961Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Glycosylation6241N-linked (GlcNAc...) Ref.9
Glycosylation6381N-linked (GlcNAc...) Ref.9

Natural variations

Natural variant7761E → D in strain: A.BY, B10.H7 and C3H.SW; correlated with B6dom1-negative phenotype. Ref.3

Experimental info

Sequence conflict431S → R in BAE41550. Ref.1
Sequence conflict431S → R in AAH03206. Ref.2
Sequence conflict2401T → I in BAE41550. Ref.1
Sequence conflict2941F → L in BAB31390. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TDQ1 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: BBC27DB07EE609D1

FASTA82393,246
        10         20         30         40         50         60 
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGTQS ASSAAAPKPG PPAGLSGGLS 

        70         80         90        100        110        120 
QPAGWQSLLS FTILFLAWLA GFSSRLFAVI RFESIIHEFD PWFNYRSTHH LASHGFYEFL 

       130        140        150        160        170        180 
NWFDERAWYP LGRIVGGTVY PGLMITAGLI HWILNTLNIT VHIRDVCVFL APTFSGLTSI 

       190        200        210        220        230        240 
STFLLTRELW NQGAGLLAAC FIAIVPGYIS RSVAGSFDNE GIAIFALQFT YYLWVKSVKT 

       250        260        270        280        290        300 
GSVFWTMCCC LSYFYMVSAW GGYVFIINLI PLHVFVLLLM QRYSKRVYIA YSTFYIVGLI 

       310        320        330        340        350        360 
LSMQIPFVGF QPIRTSEHMA AAGVFALLQA YAFLQYLRDR LTKQEFQTLF FLGVSLAAGA 

       370        380        390        400        410        420 
VFLSVIYLTY TGYIAPWSGR FYSLWDTGYA KIHIPIIASV SEHQPTTWVS FFFDLHILVC 

       430        440        450        460        470        480 
TFPAGLWFCI KNINDERVFV ALYAISAVYF AGVMVRLMLT LTPVVCMLSA IAFSNVFEHY 

       490        500        510        520        530        540 
LGDDMKRENP PVEDSSDEDD KRNPGNLYDK AGKVRKHVTE QEKPEEGLGP NIKSIVTMLM 

       550        560        570        580        590        600 
LMLLMMFAVH CTWVTSNAYS SPSVVLASYN HDGTRNILDD FREAYFWLRQ NTDEHARVMS 

       610        620        630        640        650        660 
WWDYGYQIAG MANRTTLVDN NTWNNSHIAL VGKAMSSNET AAYKIMRSLD VDYVLVIFGG 

       670        680        690        700        710        720 
VIGYSGDDIN KFLWMVRIAE GEHPKDIREG DYFTQQGEFR VDKAGSPTLL NCLMYKMSYY 

       730        740        750        760        770        780 
RFGEMQLDFR TPPGFDRTRN AEIGNKDIKF KHLEEAFTSE HWLVRIYKVK APDNRETLGH 

       790        800        810        820 
KPRVTNIVPK QKYLSKKTTK RKRGYVKNKL VFKKGKKTSK KTV

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow and Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6, Czech II and FVB/N.
Tissue: Brain, Mammary gland and Mammary tumor.
[3]"The model B6dom1 minor histocompatibility antigen is encoded by a mouse homolog of the yeast STT3 gene."
McBride K., Baron C., Picard S., Martin S., Boismenu D., Bell A., Bergeron J., Perreault C.
Immunogenetics 54:562-569(2002) [PubMed: 12439619] [Abstract]
Cited for: PROTEIN SEQUENCE OF 770-778, VARIANT ASP-776.
Strain: C57BL/6.
[4]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, MASS SPECTROMETRY.
Tissue: Liver.
[5]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, MASS SPECTROMETRY.
Tissue: Melanoma.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[9]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-624 AND ASN-638, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018758 mRNA. Translation: BAB31390.1.
AK145674 mRNA. Translation: BAE26582.1.
AK154979 mRNA. Translation: BAE32968.1.
AK152899 mRNA. Translation: BAE31580.1.
AK170079 mRNA. Translation: BAE41550.1.
BC003206 mRNA. Translation: AAH03206.1.
BC013054 mRNA. Translation: AAH13054.2. Different initiation.
BC052433 mRNA. Translation: AAH52433.1.
IPIIPI00316469.
RefSeqNP_077184.2. NM_024222.2.
UniGeneMm.296158.

3D structure databases

ProteinModelPortalQ3TDQ1.
SMRQ3TDQ1. Positions 579-682.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3TDQ1.

Protein family/group databases

CAZyGT66. Glycosyltransferase Family 66.

PTM databases

PhosphoSiteQ3TDQ1.

Proteomic databases

PRIDEQ3TDQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035010; ENSMUSP00000035010; ENSMUSG00000032437.
GeneID68292.
KEGGmmu:68292.
UCSCuc009ryp.1. mouse.

Organism-specific databases

CTD201595.
MGIMGI:1915542. Stt3b.

Phylogenomic databases

eggNOGroNOG09233.
HOGENOMHBG314442.
HOVERGENHBG010606.
InParanoidQ3TDQ1.
OrthoDBEOG4VT5WM.
PhylomeDBQ3TDQ1.

Gene expression databases

ArrayExpressQ3TDQ1.
BgeeQ3TDQ1.
GenevestigatorQ3TDQ1.
GermOnlineENSMUSG00000032437. Mus musculus.

Family and domain databases

InterProIPR003674. Oligo_trans_STT3.
[Graphical view]
KOK07151.
PfamPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio326937.
SOURCESearch...

Entry information

Entry nameSTT3B_MOUSE
AccessionPrimary (citable) accession number: Q3TDQ1
Secondary accession number(s): Q7TT24 expand/collapse secondary AC list , Q921E3, Q99LL0, Q9D2V2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: December 14, 2011
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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