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Protein

R-spondin-2

Gene

rspo2

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: Annotation score: 3 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. Acts both in the canonical. Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway. Activates neural markers and promotes muscle formation. Overexpression blocks activin, nodal and BMP4 signaling, suggesting that it may negatively regulate the TGF-beta pathway (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Wnt signaling pathway

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
R-spondin-2
Alternative name(s):
Roof plate-specific spondin-2
Gene namesi
Name:rspo2
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-946235. rspo2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 243222R-spondin-2PRO_0000234442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi196 ↔ 203PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ5M7L6.

Expressioni

Gene expression databases

BgeeiENSXETG00000003600.
ExpressionAtlasiQ5M7L6. baseline.

Interactioni

Subunit structurei

Binds heparin.By similarity

Protein-protein interaction databases

STRINGi8364.ENSXETP00000063896.

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 475Combined sources
Turni48 – 503Combined sources
Beta strandi51 – 555Combined sources
Beta strandi59 – 668Combined sources
Beta strandi69 – 779Combined sources
Beta strandi82 – 865Combined sources
Beta strandi91 – 955Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi138 – 1425Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C8VX-ray2.20A/B/C/D/E/F/G/H35-144[»]
4C8WX-ray3.10I/J35-144[»]
4C9AX-ray2.40B/D35-144[»]
4C9EX-ray3.00B/D/F/H35-144[»]
4C9RX-ray2.10B/D35-144[»]
4C9UX-ray3.00B/D35-144[»]
4C9VX-ray2.70B35-144[»]
ProteinModelPortaliQ5M7L6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati90 – 13445FUAdd
BLAST
Domaini144 – 20461TSP type-1PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiENOG410IMS2. Eukaryota.
ENOG410ZI6H. LUCA.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ5M7L6.
OMAiANRWRRS.
OrthoDBiEOG091G0FYC.
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.

Q5M7L6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFQLFSFVL IILNCVDYSH CQANRWRRSK RASYGTNPIC KGCLSCSKDN
60 70 80 90 100
GCLRCQPKLF FYLRREGMRQ YGECLQSCPP GYYGVRGPDM NRCSRCRIEN
110 120 130 140 150
CDSCFSRDFC IKCKSGFYSH KGQCFEECPE GFAPLDDTMV CVDGCEVGPW
160 170 180 190 200
SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP AKDTIPCPTI AESRRCKMAM
210 220 230 240
RHCPGGTRTT KKKDKKNKKK KKKLLERAQE QHSVVLATDR SSQ
Length:243
Mass (Da):27,937
Last modified:February 1, 2005 - v1
Checksum:i554CE54725F83E97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088569 mRNA. Translation: AAH88569.1.
RefSeqiNP_001011386.1. NM_001011386.1.
XP_012820077.1. XM_012964623.1.
UniGeneiStr.5159.

Genome annotation databases

EnsembliENSXETT00000065307; ENSXETP00000063896; ENSXETG00000003600.
GeneIDi496854.
KEGGixtr:496854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088569 mRNA. Translation: AAH88569.1.
RefSeqiNP_001011386.1. NM_001011386.1.
XP_012820077.1. XM_012964623.1.
UniGeneiStr.5159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C8VX-ray2.20A/B/C/D/E/F/G/H35-144[»]
4C8WX-ray3.10I/J35-144[»]
4C9AX-ray2.40B/D35-144[»]
4C9EX-ray3.00B/D/F/H35-144[»]
4C9RX-ray2.10B/D35-144[»]
4C9UX-ray3.00B/D35-144[»]
4C9VX-ray2.70B35-144[»]
ProteinModelPortaliQ5M7L6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8364.ENSXETP00000063896.

Proteomic databases

PaxDbiQ5M7L6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSXETT00000065307; ENSXETP00000063896; ENSXETG00000003600.
GeneIDi496854.
KEGGixtr:496854.

Organism-specific databases

CTDi340419.
XenbaseiXB-GENE-946235. rspo2.

Phylogenomic databases

eggNOGiENOG410IMS2. Eukaryota.
ENOG410ZI6H. LUCA.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ5M7L6.
OMAiANRWRRS.
OrthoDBiEOG091G0FYC.
TreeFamiTF331799.

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSXETG00000003600.
ExpressionAtlasiQ5M7L6. baseline.

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_XENTR
AccessioniPrimary (citable) accession number: Q5M7L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 1, 2005
Last modified: September 7, 2016
This is version 74 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.