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Q99P68 (SOST_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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

Names and origin

Protein namesRecommended name:
Sclerostin
Gene names
Name:Sost
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation By similarity. Ref.4

Subunit structure

Interacts with LRP4 (via the extracellular domain); the interaction facilitates the inhibition of Wnt signaling By similarity. Interacts with LRP5 (via the first two YWTD-EGF repeat domains); the interaction inhibits Wnt-mediated signaling By similarity. Interacts with LRP6 By similarity. Ref.3

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Disruption phenotype

Mice were resistant to mechanical unloading-induced bone loss. Ref.4

Sequence similarities

Belongs to the sclerostin family.

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 211188Sclerostin
PRO_0000033178

Regions

Domain80 – 17091CTCK

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 132 Ref.5
Disulfide bond92 ↔ 146 Ref.5
Disulfide bond103 ↔ 163 Ref.5
Disulfide bond107 ↔ 165 Ref.5

Experimental info

Sequence conflict721G → D in BAB30678. Ref.2
Sequence conflict721G → D in AAK13452. Ref.2

Secondary structure

........... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99P68 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AEB094E358E34961

FASTA21123,443
        10         20         30         40         50         60 
MQPSLAPCLI CLLVHAAFCA VEGQGWQAFR NDATEVIPGL GEYPEPPPEN NQTMNRAENG 

        70         80         90        100        110        120 
GRPPHHPYDA KGVSEYSCRE LHYTRFLTDG PCRSAKPVTE LVCSGQCGPA RLLPNAIGRV 

       130        140        150        160        170        180 
KWWRPNGPDF RCIPDRYRAQ RVQLLCPGGA APRSRKVRLV ASCKCKRLTR FHNQSELKDF 

       190        200        210 
GPETARPQKG RKPRPGARGA KANQAELENA Y 

« Hide

References

« Hide 'large scale' references
[1]"Bone dysplasia sclerosteosis results from loss of the SOST gene product, a novel cystine knot-containing protein."
Brunkow M.E., Gardner J.C., Van Ness J., Paeper B.W., Kovacevich B.R., Proll S., Skonier J.E., Zhao L., Sabo P.J., Fu Y.H., Alisch R.S., Gillett L., Colbert T., Tacconi P., Galas D., Hamersma H., Beighton P., Mulligan J.T.
Am. J. Hum. Genet. 68:577-589(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[3]"Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling."
Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E., Wu D.
J. Biol. Chem. 280:19883-19887(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP5 AND LRP6.
[4]"Sclerostin mediates bone response to mechanical unloading through antagonizing Wnt/beta-catenin signaling."
Lin C., Jiang X., Dai Z., Guo X., Weng T., Wang J., Li Y., Feng G., Gao X., He L.
J. Bone Miner. Res. 24:1651-1661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"NMR structure of the Wnt modulator protein Sclerostin."
Weidauer S.E., Schmieder P., Beerbaum M., Schmitz W., Oschkinat H., Mueller T.D.
Biochem. Biophys. Res. Commun. 380:160-165(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 59-167, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF326740 mRNA. Translation: AAK13455.1.
AK017295 mRNA. Translation: BAB30678.1.
AF326737 Genomic DNA. Translation: AAK13452.1.
RefSeqNP_077769.4. NM_024449.6.
UniGeneMm.265602.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KD3NMR-A59-167[»]
ProteinModelPortalQ99P68.
SMRQ99P68. Positions 71-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216800. 2 interactions.

Proteomic databases

PRIDEQ99P68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID74499.
KEGGmmu:74499.

Organism-specific databases

CTD50964.
MGIMGI:1921749. Sost.

Phylogenomic databases

eggNOGNOG40285.
HOGENOMHOG000252934.
HOVERGENHBG003729.
InParanoidQ99P68.
KOK16834.
PhylomeDBQ99P68.

Gene expression databases

CleanExMM_SOST.
GenevestigatorQ99P68.

Family and domain databases

InterProIPR008835. Sclerostin/SOSTDC1.
IPR015665. SOST.
[Graphical view]
PANTHERPTHR14903. PTHR14903. 1 hit.
PTHR14903:SF2. PTHR14903:SF2. 1 hit.
PfamPF05463. Sclerostin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ99P68.
NextBio340962.
PROQ99P68.
SOURCESearch...

Entry information

Entry nameSOST_MOUSE
AccessionPrimary (citable) accession number: Q99P68
Secondary accession number(s): Q9D3L7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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