O75462: Cytokine receptor-like factor 1 (CRLF1)

Cytokine receptor-like factor 1 (CRLF1) is a 422-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75462.

Gene
CRLF1
Organism
Homo sapiens
Length
422 residues
Mean pLDDT
80.3
Model
AF-O75462-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.3 (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 accurate56%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Functions as secretory protein carrier chaperone that promotes cellular release (PubMed:10966616). Also functions as a cytokine subunit within the CRLF1-CLCF1 heterodimer, which engages the CNTF receptor complex (CNTFR, IL6ST/gp130, LIFR) (PubMed:10966616). As part of the CRLF-CLCF1 complex, binds to CNTFR, induces dimerization of the IL6ST/gp130 and LIFR, which activates JAK tyrosine kinases (JAK1 or JAK2 and to lesser extent TYK2) bound to their intracellular domains (PubMed:11294841). These kinases subsequently phosphorylate IL6ST/gp130 and LIFR (PubMed:11294841). The tyrosine phosphorylated signaling receptors serve in turn as docking sites for recruitment and activation of signal…

Subunit structure

Homodimer (PubMed:36930708, PubMed:9686600). Tetramer (PubMed:9686600). Forms a heterotetrameric complex with CLCF1/CLC; this complex is a ligand of the ciliary neurotrophic factor (CNTF) receptor complex through CLCF1 and CNTFR binding (PubMed:10966616, PubMed:26858303, PubMed:36930708). The CRLF1-CLCF1 heterodimer binds SORL1 (via N-terminal ectodomain); within this complex, the interaction is…

Subcellular location

Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8D7HEM3.4 ÅA/E=38-422

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