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Nidogen-2; NID-2; osteonidogen (NID2)
Function:
1) cell adhesion protein
2) binds to collagen 1, collagen 4, perlecan & laminin 1
3) does not bind fibulins
4) role in cell-extracellular matrix interactions
5) interacts with LAMA2
Structure:
1) highly N-glycosylated & O-glycosylated
2) contains 5 EGF-like domains
- contains 5 LDL-receptor class B repeats
- contains 1 NIDO domain
- contains 1 nidogen G2 beta-barrel domain
- contains 2 thyroglobulin type-1 domains
Compartment:
- secreted, extracellular matrix
- widely distributed in basement membranes
Expression:
- expressed in heart, placenta, bone > pancreas, kidney, skeletal muscle
General
Ca+2 binding protein
cell adhesion protein
glycoprotein
Properties
SIZE: entity length = 1375 aa
MW = 151 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-30}
NIDO {108-273}
N-glycosylation site {N417}
EGF domain {484-524}
Nidogen G2 beta-barrel {528-758}
MOTIF: N-glycosylation site {N658}
N-glycosylation site {N693}
N-glycosylation site {N703}
EGF domain {759-800}
MOTIF: cysteine residue {C763}
MODIFICATION: cysteine residue {C776}
cysteine residue {C770}
MODIFICATION: cysteine residue {C786}
cysteine residue {C776}
MODIFICATION: cysteine residue {C763}
cysteine residue {C786}
MODIFICATION: cysteine residue {C770}
cysteine residue {C788}
MODIFICATION: cysteine residue {C799}
cysteine residue {C799}
MODIFICATION: cysteine residue {C788}
EGF domain {801-843}
MOTIF: cysteine residue {C805}
MODIFICATION: cysteine residue {C818}
cysteine residue {C812}
MODIFICATION: cysteine residue {C827}
cysteine residue {C818}
MODIFICATION: cysteine residue {C805}
cysteine residue {C827}
MODIFICATION: cysteine residue {C812}
cysteine residue {C829}
MODIFICATION: cysteine residue {C842}
cysteine residue {C842}
MODIFICATION: cysteine residue {C829}
EGF domain {848-891}
MOTIF: cysteine residue {C852}
MODIFICATION: cysteine residue {C867}
cysteine residue {C859}
MODIFICATION: cysteine residue {C877}
cysteine residue {C867}
MODIFICATION: cysteine residue {C852}
cysteine residue {C877}
MODIFICATION: cysteine residue {C859}
cysteine residue {C879}
MODIFICATION: cysteine residue {C890}
cysteine residue {C890}
MODIFICATION: cysteine residue {C879}
EGF domain {892-930}
MOTIF: cysteine residue {C896}
MODIFICATION: cysteine residue {C907}
cysteine residue {C901}
MODIFICATION: cysteine residue {C916}
cysteine residue {C907}
MODIFICATION: cysteine residue {C896}
cysteine residue {C916}
MODIFICATION: cysteine residue {C901}
cysteine residue {C918}
MODIFICATION: cysteine residue {C929}
cysteine residue {C929}
MODIFICATION: cysteine residue {C918}
Thyroglobulin type-1 1 {937-1005}
MOTIF: cysteine residue {C940}
MODIFICATION: cysteine residue {C963}
cysteine residue {C963}
MODIFICATION: cysteine residue {C940}
cysteine residue {C974}
MODIFICATION: cysteine residue {C981}
cysteine residue {C981}
MODIFICATION: cysteine residue {C974}
cysteine residue {C983}
MODIFICATION: cysteine residue {C1005}
cysteine residue {C1005}
MODIFICATION: cysteine residue {C983}
Thyroglobulin type-1 2 {1016-1084}
MOTIF: cysteine residue {C1019}
MODIFICATION: cysteine residue {C1043}
cysteine residue {C1043}
MODIFICATION: cysteine residue {C1019}
cysteine residue {C1054}
MODIFICATION: cysteine residue {C1061}
cysteine residue {C1061}
MODIFICATION: cysteine residue {C1054}
cysteine residue {C1063}
MODIFICATION: cysteine residue {C1084}
cysteine residue {C1084}
MODIFICATION: cysteine residue {C1063}
N-glycosylation site {N1124}
LDL-receptor class B {1154-1197}
LDL-receptor class B {1198-1240}
LDL-receptor class B {1241-1285}
LDL-receptor class B {1286-1327}
LDL-receptor class B {1329-1373}
Database Correlations
OMIM 605399
UniProt Q14112
PFAM correlations
Entrez Gene 22795
Kegg hsa:22795
References
UniProt :accession Q14112