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Q8BFU0

- RSPO2_MOUSE

UniProt

Q8BFU0 - RSPO2_MOUSE

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Protein
R-spondin-2
Gene
Rspo2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. heparin binding Source: MGI

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. bone mineralization Source: MGI
  3. embryonic forelimb morphogenesis Source: MGI
  4. embryonic hindlimb morphogenesis Source: MGI
  5. epithelial tube branching involved in lung morphogenesis Source: MGI
  6. lung growth Source: MGI
  7. osteoblast differentiation Source: MGI
  8. positive regulation of canonical Wnt signaling pathway Source: MGI
  9. trachea cartilage morphogenesis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Wnt signaling pathway

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_213035. regulation of FZD by ubiquitination.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Rspo2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1922667. Rspo2.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. cell surface Source: MGI
  2. extracellular region Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 243220R-spondin-2
PRO_0000234440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 46 By similarity
Disulfide bondi43 ↔ 52 By similarity
Disulfide bondi55 ↔ 74 By similarity
Disulfide bondi78 ↔ 93 By similarity
Disulfide bondi96 ↔ 104 By similarity
Disulfide bondi101 ↔ 110 By similarity
Disulfide bondi113 ↔ 124 By similarity
Disulfide bondi128 ↔ 141 By similarity
Disulfide bondi145 ↔ 187 By similarity
Disulfide bondi156 ↔ 163 By similarity
Glycosylationi160 – 1601N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi196 ↔ 203 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8BFU0.

PTM databases

PhosphoSiteiQ8BFU0.

Expressioni

Developmental stagei

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).1 Publication

Gene expression databases

BgeeiQ8BFU0.
CleanExiMM_RSPO2.
GenevestigatoriQ8BFU0.

Interactioni

Subunit structurei

Interacts with WNT1. Binds heparin. Interacts with LGR4, LGR5 and LGR6.2 Publications

Protein-protein interaction databases

BioGridi232079. 2 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453
Turni48 – 503
Beta strandi51 – 555
Beta strandi59 – 668
Beta strandi69 – 779
Beta strandi105 – 1084
Beta strandi118 – 1203
Beta strandi123 – 1275
Turni136 – 1383

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C99X-ray2.80B/D37-144[»]
ProteinModelPortaliQ8BFU0.
SMRiQ8BFU0. Positions 39-143.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati90 – 13445FU
Add
BLAST
Domaini144 – 20461TSP type-1
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the R-spondin family.
Contains 1 TSP type-1 domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG285562.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ8BFU0.
OMAiDNGCIRC.
OrthoDBiEOG7X9G7G.
PhylomeDBiQ8BFU0.
TreeFamiTF331799.

Family and domain databases

InterProiIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
SMARTiSM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEiPS50092. TSP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BFU0-1 [UniParc]FASTAAdd to Basket

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MRFCLFSFAL IILNCMDYSQ CQGNRWRRNK RASYVSNPIC KGCLSCSKDN    50
GCSRCQQKLF FFLRREGMRQ YGECLHSCPS GYYGHRAPDM NRCARCRIEN 100
CDSCFSKDFC TKCKVGFYLH RGRCFDECPD GFAPLDETME CVEGCEVGHW 150
SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP AKDTIPCPTI AESRRCKMAM 200
RHCPGGKRTP KAKEKRNKKK RRKLIERAQE QHSVFLATDR VNQ 243
Length:243
Mass (Da):28,276
Last modified:March 1, 2003 - v1
Checksum:iED76A08D61012ED7
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049891 mRNA. Translation: BAC33974.1.
AK087485 mRNA. Translation: BAC39893.1.
BC052844 mRNA. No translation available.
CCDSiCCDS27451.1.
RefSeqiNP_766403.1. NM_172815.3.
XP_006520968.1. XM_006520905.1.
UniGeneiMm.193274.

Genome annotation databases

EnsembliENSMUST00000063492; ENSMUSP00000067325; ENSMUSG00000051920.
GeneIDi239405.
KEGGimmu:239405.
UCSCiuc007vpg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049891 mRNA. Translation: BAC33974.1 .
AK087485 mRNA. Translation: BAC39893.1 .
BC052844 mRNA. No translation available.
CCDSi CCDS27451.1.
RefSeqi NP_766403.1. NM_172815.3.
XP_006520968.1. XM_006520905.1.
UniGenei Mm.193274.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4C99 X-ray 2.80 B/D 37-144 [» ]
ProteinModelPortali Q8BFU0.
SMRi Q8BFU0. Positions 39-143.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232079. 2 interactions.

PTM databases

PhosphoSitei Q8BFU0.

Proteomic databases

PRIDEi Q8BFU0.

Protocols and materials databases

DNASUi 239405.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063492 ; ENSMUSP00000067325 ; ENSMUSG00000051920 .
GeneIDi 239405.
KEGGi mmu:239405.
UCSCi uc007vpg.1. mouse.

Organism-specific databases

CTDi 340419.
MGIi MGI:1922667. Rspo2.

Phylogenomic databases

eggNOGi NOG285562.
GeneTreei ENSGT00390000011447.
HOGENOMi HOG000290668.
HOVERGENi HBG082751.
InParanoidi Q8BFU0.
OMAi DNGCIRC.
OrthoDBi EOG7X9G7G.
PhylomeDBi Q8BFU0.
TreeFami TF331799.

Enzyme and pathway databases

Reactomei REACT_213035. regulation of FZD by ubiquitination.

Miscellaneous databases

NextBioi 384105.
PROi Q8BFU0.
SOURCEi Search...

Gene expression databases

Bgeei Q8BFU0.
CleanExi MM_RSPO2.
Genevestigatori Q8BFU0.

Family and domain databases

InterProi IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
SMARTi SM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEi PS50092. TSP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRSPO2_MOUSE
AccessioniPrimary (citable) accession number: Q8BFU0
Secondary accession number(s): Q7TPX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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