testican-1 (sparc/osteonectin, cwcv, & kazal-like domains proteoglycan; protein SPOCK; SPOCK1; SPOCK; TIC1; TICN1)

Function: 1) role in cell-cell & cell-matrix interactions (putative) 2) role in neuronal mechanisms in the central nervous system (putative) Structure: - contains chondroitin sulfate & heparan sulfate O-linked oligosaccharides. - contains 1 Kazal-like domain - contains 1 thyroglobulin type-1 domain Compartment: secreted, extracellular matrix

Properties

SIZE: MW = 49 kD entity length = 439 aa MOTIF: signal sequence {1-21} cysteine residue {C86} MODIFICATION: cysteine residue {C97} cysteine residue {C91} MODIFICATION: cysteine residue {C107} cysteine residue {C97} MODIFICATION: cysteine residue {C86} cysteine residue {C107} MODIFICATION: cysteine residue {C91} Kazal-type serine protease inhibitor domain {136-180} 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} cysteine residue {C136} MODIFICATION: cysteine residue {C166} cysteine residue {C139} MODIFICATION: cysteine residue {C159} cysteine residue {C148} MODIFICATION: cysteine residue {C180} cysteine residue {C159} MODIFICATION: cysteine residue {C139} cysteine residue {C166} MODIFICATION: cysteine residue {C136} cysteine residue {C180} MODIFICATION: cysteine residue {C148} FOR-BINDING-OF: serine protease Thyroglobulin type-1 {310-376} MOTIF: cysteine residue {C313} MODIFICATION: cysteine residue {C337} cysteine residue {C337} MODIFICATION: cysteine residue {C313} cysteine residue {C348} MODIFICATION: cysteine residue {C355} cysteine residue {C355} MODIFICATION: cysteine residue {C348} cysteine residue {C357} MODIFICATION: cysteine residue {C376} cysteine residue {C376} MODIFICATION: cysteine residue {C357} Ser glycosylation site {S383} Ser glycosylation site {S388}

Database Correlations

OMIM 602264 UniProt Q08629 PFAM correlations

References

UniProt :accession Q08629