Contents

Search


testican-2 (SPARC/osteonectin, CWCV, & Kazal-like domains proteoglycan 2, SPOCK2, KIAA0275, TICN2, UNQ269/PRO306)

Function: 1) may participate in diverse steps of neurogenesis 2) binds Ca+2 Compartment: extracellular matrix Expression: - expressed in brain > lung, testis Structure: - contains chondroitin sulfate & heparan sulfate O-linked oligosaccharides - contains 1 Kazal-like domain - contains 1 thyroglobulin type-1 domain

General

glycoprotein secreted protein

Properties

SIZE: MW = 47 kD entity length = 424 aa COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-22} cysteine residue {C90} MODIFICATION: cysteine residue {C101} cysteine residue {C95} MODIFICATION: cysteine residue {C111} cysteine residue {C101} MODIFICATION: cysteine residue {C90} cysteine residue {C111} MODIFICATION: cysteine residue {C95} 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 N-glycosylation site {N225} 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} glutamate-rich region {393-416} MOTIF: glutamate residue (SEVERAL)

Database Correlations

OMIM 607988 UniProt Q92563 PFAM correlations

References

UniProt :accession Q92563