CRLF1

Functions as secretory protein carrier chaperone that promotes cellular release. Also functions as a cytokine subunit within the CRLF1-CLCF1 heterodimer, which engages the CNTF receptor complex (CNTFR, IL6ST/gp130, LIFR). 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. These kinases subsequently phosphorylate IL6ST/gp130 and LIFR. The tyrosine phosphorylated signaling receptors serve in turn as docking sites for recruitment and activation of signal transducer and activators of transcription (STAT3 and to lesser extent STAT1). Moreover, CLCF1/CLF heterodimer induces tyrosine phosphorylation of PTPN11, that associates with IL6ST/gp130-LIFR, which in turn recruits PIK3 protein kinase followed by AKT protein phosphorylation. Participates in the survival of embryonic motor neurons. May also play a regulatory role in the immune system..

Function from UniProtKB (O75462), read 2026-09-23. CC BY 4.0.