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Q8BFU0 (RSPO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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:
R-spondin-2
Alternative name(s):
Cysteine-rich and single thrombospondin domain-containing protein 2
Short name=Cristin-2
Short name=mCristin-2
Roof plate-specific spondin-2
Gene names
Name:Rspo2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Probably also acts as a ligand for frizzled and LRP receptors. Ref.5

Subunit structure

Interacts with WNT1. Binds heparin. Interacts with LGR4, LGR5 and LGR6. Ref.4 Ref.5

Subcellular location

Secreted Ref.4.

Developmental stage

Detected from day 9.5 in various neural and mesodermal derivatives, mainly along diencephalon. Strongly expressed in limb buds, particularly in the morphogenetically active region such as the apical ectodermal ridge (AER). Ref.3

Domain

The FU repeat is required for activation and stabilization of beta-catenin By similarity.

Sequence similarities

Belongs to the R-spondin family.

Contains 1 FU (furin-like) repeat.

Contains 1 TSP type-1 domain.

Sequence caution

The sequence BC052844 differs from that shown. Reason: Erroneous termination at position 153. Translated as Trp.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 243220R-spondin-2
PRO_0000234440

Regions

Repeat90 – 13445FU
Domain144 – 20461TSP type-1

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 46 By similarity
Disulfide bond43 ↔ 52 By similarity
Disulfide bond55 ↔ 74 By similarity
Disulfide bond78 ↔ 93 By similarity
Disulfide bond96 ↔ 104 By similarity
Disulfide bond101 ↔ 110 By similarity
Disulfide bond113 ↔ 124 By similarity
Disulfide bond128 ↔ 141 By similarity
Disulfide bond145 ↔ 187 By similarity
Disulfide bond156 ↔ 163 By similarity
Disulfide bond196 ↔ 203 By similarity

Secondary structure

.................. 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8BFU0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: ED76A08D61012ED7

FASTA24328,276
        10         20         30         40         50         60 
MRFCLFSFAL IILNCMDYSQ CQGNRWRRNK RASYVSNPIC KGCLSCSKDN GCSRCQQKLF 

        70         80         90        100        110        120 
FFLRREGMRQ YGECLHSCPS GYYGHRAPDM NRCARCRIEN CDSCFSKDFC TKCKVGFYLH 

       130        140        150        160        170        180 
RGRCFDECPD GFAPLDETME CVEGCEVGHW SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP 

       190        200        210        220        230        240 
AKDTIPCPTI AESRRCKMAM RHCPGGKRTP KAKEKRNKKK RRKLIERAQE QHSVFLATDR 


VNQ 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye and Hippocampus.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Egg.
[3]"R-Spondin2 is a secreted activator of Wnt/beta-catenin signaling and is required for Xenopus myogenesis."
Kazanskaya O., Glinka A., del Barco Barrantes I., Stannek P., Niehrs C., Wu W.
Dev. Cell 7:525-534(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[4]"Mouse cristin/R-spondin family proteins are novel ligands for the Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent gene expression."
Nam J.-S., Turcotte T.J., Smith P.F., Choi S., Yoon J.K.
J. Biol. Chem. 281:13247-13257(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, HEPARIN-BINDING, INTERACTION WITH WNT1.
[5]"R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling."
Carmon K.S., Gong X., Lin Q., Thomas A., Liu Q.
Proc. Natl. Acad. Sci. U.S.A. 108:11452-11457(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGR4 AND LGR5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK049891 mRNA. Translation: BAC33974.1.
AK087485 mRNA. Translation: BAC39893.1.
BC052844 mRNA. No translation available.
RefSeqNP_766403.1. NM_172815.3.
XP_006520968.1. XM_006520905.1.
UniGeneMm.193274.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4C99X-ray2.80B/D37-144[»]
ProteinModelPortalQ8BFU0.
SMRQ8BFU0. Positions 39-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid232079. 2 interactions.

PTM databases

PhosphoSiteQ8BFU0.

Proteomic databases

PRIDEQ8BFU0.

Protocols and materials databases

DNASU239405.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063492; ENSMUSP00000067325; ENSMUSG00000051920.
GeneID239405.
KEGGmmu:239405.
UCSCuc007vpg.1. mouse.

Organism-specific databases

CTD340419.
MGIMGI:1922667. Rspo2.

Phylogenomic databases

eggNOGNOG285562.
GeneTreeENSGT00390000011447.
HOGENOMHOG000290668.
HOVERGENHBG082751.
InParanoidQ8BFU0.
OMADNGCIRC.
OrthoDBEOG7X9G7G.
PhylomeDBQ8BFU0.
TreeFamTF331799.

Gene expression databases

BgeeQ8BFU0.
CleanExMM_RSPO2.
GenevestigatorQ8BFU0.

Family and domain databases

InterProIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
SMARTSM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEPS50092. TSP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384105.
PROQ8BFU0.
SOURCESearch...

Entry information

Entry nameRSPO2_MOUSE
AccessionPrimary (citable) accession number: Q8BFU0
Secondary accession number(s): Q7TPX3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 84 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