Q9UBD9: Cardiotrophin-like cytokine factor 1 (CLCF1)

Cardiotrophin-like cytokine factor 1 (CLCF1) is a 225-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBD9.

Gene
CLCF1
Organism
Homo sapiens
Length
225 residues
Mean pLDDT
81.6
Model
AF-Q9UBD9-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.6 (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 accurate57%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Functions as a cytokine, either alone or by forming a stable complex with soluble CRLF1 or CNTFR (PubMed:10448081, PubMed:10500198, PubMed:10966616, PubMed:11285233, PubMed:11294841). Binds to CNTFR complex (CNTFR, IL6ST/gp130, LIFR) or can signal via trans-signaling using soluble CNTFR subunits (PubMed:10966616, PubMed:11285233, PubMed:11294841). Mechanistically, ligand binding 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, PubMed:16782820). These kinases subsequently phosphorylate IL6ST/gp130 and LIFR (PubMed:11294841). The tyrosine…

Subunit structure

Homodimer (PubMed:36930708). Forms a heterotetrameric complex with CRLF1/CLF-1; 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 interacts with SORL1 (via Vps10p domain); within this complex, the interaction is mediated predominantly by the CRLF1…

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 ÅD/H=28-225
8D7REM3.9 ÅD=28-225

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