Q969F8: KiSS-1 receptor (KISS1R)

KiSS-1 receptor (KISS1R) is a 398-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q969F8.

Gene
KISS1R
Organism
Homo sapiens
Length
398 residues
Mean pLDDT
75.3
Model
AF-Q969F8-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.3 (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 accurate33%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Receptor for kisspeptins (kisspeptin-10, kisspeptin-13, kisspeptin-14 and metastin/kisspeptin-54) (PubMed:11457843, PubMed:11527393, PubMed:15020672, PubMed:15596153). The hypothalamic KISS1/KISS1R signaling system plays a central role in the regulation of the hypothalamic-pituitary-gonadal reproductive axis by modulating the secretion of gonadotropin-releasing hormone (GnRH) from GnRH neurons (PubMed:12944565, PubMed:14573733, PubMed:15598687, PubMed:17164310, PubMed:18272894). In these neurons, kisspeptin binding to its receptor activates G(q)-dependent signaling, leading to phospholipase C (PLC) activation, and hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) (PubMed:14573733,…

Subunit structure

Interacts with SRC and DUSP18; the interaction depends on receptor activation by kisspeptin-10 and is required for DUSP18-mediated dephosphorylation of SRC (PubMed:38346942). Interaction with SRC and DUSP18 is relevant for down-regulation of osteoclast differentiation and activity, and consequently suppression of bone resorption (By similarity)

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8XGOEM2.68 ÅA=1-398
8XGSEM2.95 ÅA=1-398
8XGUEM3.0 ÅA=1-398
8ZJDEM3.06 ÅR=2-355
8ZJEEM3.07 ÅR=1-398
7YQEX-ray3.5 ÅA/B=333-357

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