Q2MKA7: R-spondin-1 (RSPO1)

R-spondin-1 (RSPO1) is a 263-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q2MKA7.

Gene
RSPO1
Organism
Homo sapiens
Length
263 residues
Mean pLDDT
74.7
Model
AF-Q2MKA7-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.7 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate40%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors (PubMed:29769720). 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. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Regulates Wnt…

Subunit structure

Interacts with the extracellular domain of FZD8 and LRP6. It however does not form a ternary complex with FZD8 and LRP6. Interacts with WNT1. Binds heparin (By similarity). Interacts with ZNRF3; promoting indirect interaction between ZNRF3 and LGR4 and membrane clearance of ZNRF3. Interacts with LGR4, LGR5 and LGR6. Identified in a complex composed of RNF43, LGR5 and RSPO1. Interacts (via FU…

Subcellular location

Secreted, Nucleus

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
4BSPX-ray2.0 ÅA=31-146
4BSOX-ray2.2 ÅA=31-146
4QXFX-ray2.25 ÅC/E=34-135
4KNGX-ray2.5 ÅM/P=35-144
4KT1X-ray2.5 ÅE=39-128
4CDKX-ray2.8 ÅE/F/G/H=31-145
4LI2X-ray3.19 ÅB=33-144
4BSRX-ray3.2 ÅC/D=31-146
4BSSX-ray3.2 ÅC/D/G/H=31-146
4BSUX-ray3.2 ÅC/D/G/H=31-146
8WVUEM3.61 ÅB=35-144
4BSTX-ray4.3 ÅC/D=31-146

More AlphaFold highlights

About this viewer

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