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SPARC-related modular calcium-binding protein 1 (secreted modular calcium-binding protein 1, SMOC-1, SMOC1)

Structure: glycosylated Compartment: - secreted, extracellular matrix, basement membrane Alternative splicing: named isoforms=2 Expression: - widely expressed in many tissues - strongest signal in ovary - no expression in spleen

Related

SPARC-related modular calcium-binding protein 2 (secreted modular calcium-binding protein 2, SMOC-2, smooth muscle-associated protein 2, SMAP-2, SMOC2, SMAP2, MSTP117)

General

Ca+2 binding protein glycoprotein secreted protein

Properties

SIZE: MW = 48 kD entity length = 434 aa COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-26} Kazal-type serine protease inhibitor domain {43-87} MOTIF: cysteine residue {X+0} MODIFICATION: cysteine residue {X+X4} cysteine residue {X+X1} MODIFICATION: cysteine residue {X+X3} cysteine residue {X+X2} MODIFICATION: cysteine residue {X+X5} cysteine residue {X+X3} MODIFICATION: cysteine residue {X+X1} cysteine residue {X+X4} MODIFICATION: cysteine residue {X+0} cysteine residue {X+X5} MODIFICATION: cysteine residue {X+X2} FOR-BINDING-OF: serine protease thyroglobulin type 1 {92-158} MOTIF: cysteine residue {C95} MODIFICATION: cysteine residue {C118} cysteine residue {C118} MODIFICATION: cysteine residue {C95} cysteine residue {C129} MODIFICATION: cysteine residue {C136} cysteine residue {C136} MODIFICATION: cysteine residue {C129} cysteine residue {C138} MODIFICATION: cysteine residue {C158} cysteine residue {C158} MODIFICATION: cysteine residue {C138} N-glycosylation site {N214} thyroglobulin type 1 {224-292} MOTIF: cysteine residue {C227} MODIFICATION: cysteine residue {C251} cysteine residue {C251} MODIFICATION: cysteine residue {C227} cysteine residue {C262} MODIFICATION: cysteine residue {C269} cysteine residue {C269} MODIFICATION: cysteine residue {C262} cysteine residue {C271} MODIFICATION: cysteine residue {C292} cysteine residue {C292} MODIFICATION: cysteine residue {C271} EF hand SITE: 359-394 MOTIF: N-glycosylation site {N374} EF hand SITE: 396-431

Database Correlations

UniProt Q9H4F8 PFAM correlations

References

UniProt :accession Q9H4F8