secreted frizzled-related protein 4; sFRP-4; Frizzled protein, human endometrium; FrpHE (SFRP4, FRPHE)

Function: - soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts - they have a role in regulating cell growth & differentiation in specific cell types - SFRP4 may act as a regulator of adult uterine morphology & function - increases apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling - has phosphaturic effects by specifically inhibiting Na⁺-dependent phosphate uptake Structure: - the FZ domain is involved in binding with Wnt ligands - belongs to the secreted frizzled-related protein (sFRP) family - contains 1 FZ (frizzled) domain - contains 1 NTR domain Compartment: - secreted - cytoplasmic in ovarian tumorcells Expression: - expressed in mesenchymal cells - highly expressed in the stroma of proliferative endometrium - expressed in cardiomyocytes Pathology: - moderate to strong expression in ovarian tumors with expression increasing as the tumor stage increases - in ovarian tumors, expression levels are inversely correlated with expression of CTNNB1 (at protein level) - increased levels in failing myocardium - up-regulated in several tumor types including ostomalacia- associated tumors, endometrial cancer & breast cancer

Properties

SIZE: entity length = 346 aa MW = 40 kD COMPARTMENT: cytoplasm MOTIF: signal sequence {1-18} frizzled domain {19-139} MOTIF: cysteine residue {C24} MODIFICATION: cysteine residue {C85} cysteine residue {C32} MODIFICATION: cysteine residue {C78} N-glycosylation site {N38} N-glycosylation site {N68} cysteine residue {C69} MODIFICATION: cysteine residue {C108} cysteine residue {C78} MODIFICATION: cysteine residue {C32} cysteine residue {C85} MODIFICATION: cysteine residue {C24} cysteine residue {C97} MODIFICATION: cysteine residue {C136} cysteine residue {C101} MODIFICATION: cysteine residue {C125} cysteine residue {C108} MODIFICATION: cysteine residue {C69} N-glycosylation site {N116} cysteine residue {C125} MODIFICATION: cysteine residue {C101} cysteine residue {C136} MODIFICATION: cysteine residue {C97} NTR {178-307} MOTIF: N-glycosylation site {N194} N-glycosylation site {N240}

Database Correlations

OMIM 606570 UniProt Q6FHJ7 PFAM correlations Entrez Gene 6424 Kegg hsa:6424

References

UniProt :accession Q6FHJ7