frizzled-8; Fz-8; hFz8 (FZD8)

Function: - receptor for Wnt proteins - most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin & activation of Wnt target genes - a second signaling pathway involving PKC & Ca⁺² fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase - both pathways seem to involve interactions with G-proteins - may be involved in transduction & intercellular transmission of polarity information during tissue morphogenesis &/or in differentiated tissues - interacts with GOPC - interacts with RSPO1 & RSPO3 - ryk tyrosine kinase receptor Structure: - the PDZ-binding motif mediates interaction with GOPC - Lys-Thr-X-X-X-Trp motif is involved in the activation of the Wnt/beta-catenin signaling pathway (putative) - FZ domain is involved in binding with Wnt ligands - belongs to the G-protein coupled receptor Fz/smo family - contains 1 FZ (frizzled) domain Compartment: - membrane Expression: - most abundant in fetal kidney, followed by brain & lung - in adults, expressed in kidney, heart, pancreas & skeletal muscle

General

frizzled homolog protein glycoprotein

Properties

SIZE: entity length = 694 aa MW = 73 kD COMPARTMENT: cellular membrane MOTIF: exoplasmic domain {1-275} MOTIF: signal sequence {1-27} frizzled domain {30-151} cysteine residue {C35} MODIFICATION: cysteine residue {C96} cysteine residue {C43} MODIFICATION: cysteine residue {C89} N-glycosylation site {N49} cysteine residue {C80} MODIFICATION: cysteine residue {C118} cysteine residue {C89} MODIFICATION: cysteine residue {C43} cysteine residue {C96} MODIFICATION: cysteine residue {C35} cysteine residue {C107} MODIFICATION: cysteine residue {C148} cysteine residue {C111} MODIFICATION: cysteine residue {C135} cysteine residue {C118} MODIFICATION: cysteine residue {C80} cysteine residue {C135} MODIFICATION: cysteine residue {C111} cysteine residue {C148} MODIFICATION: cysteine residue {C107} N-glycosylation site {N152} proline-rich region SITE: 168-172 MOTIF: proline residue (SEVERAL) glycine-rich region {194-202} glycine-rich region {211-216} transmembrane domain {276-296} cytoplasmic loop {297-312} transmembrane domain {313-333} exoplasmic loop {334-396} transmembrane domain {397-417} cytoplasmic loop {418-439} transmembrane domain {440-460} exoplasmic loop {461-483} MOTIF: N-glycosylation site {N475} transmembrane domain {484-504} cytoplasmic loop {505-532} transmembrane domain {533-553} exoplasmic loop {554-584} transmembrane domain {585-605} cytoplasmic domain {606-694} MOTIF: Lys-Thr-X-X-X-Trp {608-613} glycine-rich region {639-663} PDZ recognition motif NAME: PDZ recognition motif SITE: 692-694 FOR-BINDING-VIA: PDZ domain

Database Correlations

OMIM 606146 UniProt Q9H461 PFAM correlations Entrez Gene 8325 Kegg hsa:8325