frizzled-1; Fz-1; hFz1; FzE1 (FZD1)

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 - activated by Wnt3A, Wnt3, Wnt1 & to a lesser extent Wnt2, - not activated by Wnt4, Wnt5A, Wnt5B, Wnt6, Wnt7A or Wnt7B - - binds to LRP1 which leads to repression of canonical wnt signaling Structure: - 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: - expressed in adult heart, placenta, lung, kidney, pancreas, prostate, & ovary & in fetal lung & kidney

General

frizzled homolog protein glycoprotein

Properties

SIZE: entity length = 647 aa MW = 71 kD COMPARTMENT: cellular membrane MOTIF: exoplasmic domain {1-322} MOTIF: signal sequence {1-69} proline-rich region SITE: 89-93 MOTIF: proline residue (SEVERAL) frizzled domain {111-230} cysteine residue {C116} MODIFICATION: cysteine residue {C177} cysteine residue {C124} MODIFICATION: cysteine residue {C170} N-glycosylation site {N130} cysteine residue {C161} MODIFICATION: cysteine residue {C198} cysteine residue {C170} MODIFICATION: cysteine residue {C124} cysteine residue {C177} MODIFICATION: cysteine residue {C116} cysteine residue {C187} MODIFICATION: cysteine residue {C227} cysteine residue {C191} MODIFICATION: cysteine residue {C215} cysteine residue {C198} MODIFICATION: cysteine residue {C161} cysteine residue {C215} MODIFICATION: cysteine residue {C191} cysteine residue {C227} MODIFICATION: cysteine residue {C187} N-glycosylation site {N231} transmembrane domain {323-343} cytoplasmic loop {344-354} transmembrane domain {355-375} exoplasmic loop {376-402} transmembrane domain {403-423} cytoplasmic loop {424-445} transmembrane domain {446-466} exoplasmic loop {467-489} transmembrane domain {490-510} cytoplasmic loop {511-536} transmembrane domain {537-557} exoplasmic loop {558-601} transmembrane domain {602-622} cytoplasmic domain {623-647} MOTIF: Lys-Thr-X-X-X-Trp {625-630} PDZ recognition motif NAME: PDZ recognition motif SITE: 645-647 FOR-BINDING-VIA: PDZ domain

Database Correlations

OMIM 603408 UniProt Q9UP38 PFAM correlations Entrez Gene 8321 Kegg hsa:8321