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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