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Protein

R-spondin-2

Gene

Rspo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • heparin binding Source: MGI
  • receptor binding Source: MGI

GO - Biological processi

  • bone mineralization Source: MGI
  • dopaminergic neuron differentiation Source: MGI
  • embryonic forelimb morphogenesis Source: MGI
  • embryonic hindlimb morphogenesis Source: MGI
  • epithelial tube branching involved in lung morphogenesis Source: MGI
  • lung growth Source: MGI
  • negative regulation of odontogenesis of dentin-containing tooth Source: MGI
  • osteoblast differentiation Source: MGI
  • positive regulation of canonical Wnt signaling pathway Source: MGI
  • trachea cartilage morphogenesis Source: MGI
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Wnt signaling pathway

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-MMU-4641263. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1922667. Rspo2.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular region Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000023444024 – 243R-spondin-2Add BLAST220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 46PROSITE-ProRule annotation
Disulfide bondi43 ↔ 52PROSITE-ProRule annotation
Disulfide bondi55 ↔ 74PROSITE-ProRule annotation
Disulfide bondi78 ↔ 93PROSITE-ProRule annotation
Disulfide bondi96 ↔ 104PROSITE-ProRule annotation
Disulfide bondi101 ↔ 110PROSITE-ProRule annotation
Disulfide bondi113 ↔ 124PROSITE-ProRule annotation
Disulfide bondi128 ↔ 141PROSITE-ProRule annotation
Disulfide bondi145 ↔ 187PROSITE-ProRule annotation
Disulfide bondi156 ↔ 163PROSITE-ProRule annotation
Glycosylationi160N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi196 ↔ 203PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8BFU0.
PeptideAtlasiQ8BFU0.
PRIDEiQ8BFU0.

PTM databases

iPTMnetiQ8BFU0.
PhosphoSitePlusiQ8BFU0.

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

BgeeiENSMUSG00000051920.
CleanExiMM_RSPO2.
GenevisibleiQ8BFU0. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi232079. 3 interactors.
STRINGi10090.ENSMUSP00000067325.

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 45Combined sources3
Beta strandi48 – 55Combined sources8
Beta strandi59 – 65Combined sources7
Beta strandi67 – 77Combined sources11
Beta strandi82 – 87Combined sources6
Beta strandi90 – 95Combined sources6
Beta strandi101 – 106Combined sources6
Beta strandi109 – 113Combined sources5
Beta strandi118 – 120Combined sources3
Beta strandi123 – 127Combined sources5
Turni136 – 139Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C99X-ray2.80B/D37-144[»]
4UFRX-ray2.20B/D39-144[»]
4UFSX-ray4.80B39-144[»]
ProteinModelPortaliQ8BFU0.
SMRiQ8BFU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati90 – 134FUAdd BLAST45
Domaini144 – 204TSP type-1PROSITE-ProRule annotationAdd BLAST61

Domaini

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

Sequence similaritiesi

Belongs to the R-spondin family.Curated
Contains 1 FU (furin-like) repeat.Curated
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KCR4. Eukaryota.
ENOG410ZI6H. LUCA.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ8BFU0.
OMAiANRWRRS.
OrthoDBiEOG091G0FYC.
PhylomeDBiQ8BFU0.
TreeFamiTF331799.

Family and domain databases

InterProiIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF15913. Furin-like_2. 1 hit.
[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

« Hide

        10         20         30         40         50
MRFCLFSFAL IILNCMDYSQ CQGNRWRRNK RASYVSNPIC KGCLSCSKDN
60 70 80 90 100
GCSRCQQKLF FFLRREGMRQ YGECLHSCPS GYYGHRAPDM NRCARCRIEN
110 120 130 140 150
CDSCFSKDFC TKCKVGFYLH RGRCFDECPD GFAPLDETME CVEGCEVGHW
160 170 180 190 200
SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP AKDTIPCPTI AESRRCKMAM
210 220 230 240
RHCPGGKRTP KAKEKRNKKK RRKLIERAQE QHSVFLATDR VNQ
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.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C99X-ray2.80B/D37-144[»]
4UFRX-ray2.20B/D39-144[»]
4UFSX-ray4.80B39-144[»]
ProteinModelPortaliQ8BFU0.
SMRiQ8BFU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232079. 3 interactors.
STRINGi10090.ENSMUSP00000067325.

PTM databases

iPTMnetiQ8BFU0.
PhosphoSitePlusiQ8BFU0.

Proteomic databases

PaxDbiQ8BFU0.
PeptideAtlasiQ8BFU0.
PRIDEiQ8BFU0.

Protocols and materials databases

DNASUi239405.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi340419.
MGIiMGI:1922667. Rspo2.

Phylogenomic databases

eggNOGiENOG410KCR4. Eukaryota.
ENOG410ZI6H. LUCA.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ8BFU0.
OMAiANRWRRS.
OrthoDBiEOG091G0FYC.
PhylomeDBiQ8BFU0.
TreeFamiTF331799.

Enzyme and pathway databases

ReactomeiR-MMU-4641263. Regulation of FZD by ubiquitination.

Miscellaneous databases

PROiQ8BFU0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000051920.
CleanExiMM_RSPO2.
GenevisibleiQ8BFU0. MM.

Family and domain databases

InterProiIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF15913. Furin-like_2. 1 hit.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 107 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

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.