Contents

Search

nidogen-1; NID-1; entactin (NID1, NID)

Function: - sulfated glycoprotein widely distributed in basement membranes & tightly associated with laminin - also binds to collagen 4 & perlecan - probably has a role in cell-extracellular matrix interactions - interacts with FBLN1 & LGALS3BP (putative) - interacts with PLXDC1 Structure: - N-glycosylated & O-glycosylated - contains 6 EGF-like domains - contains 4 LDL-receptor class B repeats - contains 1 NIDO domain - contains 1 nidogen G2 beta-barrel domain - contains 1 thyroglobulin type-1 domain Compartment: - secreted, extracellular space, extracellular matrix, basement membrane Alternative splicing: named isoforms=2

Related

Nidogen-2; NID-2; osteonidogen (NID2)

General

glycoprotein matrix protein

Properties

SIZE: entity length = 1247 aa MW = 136 kD COMPARTMENT: basal lamina MOTIF: signal sequence {1-28} NIDO {106-268} EGF domain {386-426} MOTIF: cysteine residue {C390} MODIFICATION: cysteine residue {C403} cysteine residue {C397} MODIFICATION: cysteine residue {C412} cysteine residue {C403} MODIFICATION: cysteine residue {C390} cysteine residue {C411} MODIFICATION: cysteine residue {C618} cysteine residue {C412} MODIFICATION: cysteine residue {C397} cysteine residue {C414} MODIFICATION: cysteine residue {C425} cysteine residue {C425} MODIFICATION: cysteine residue {C414} Nidogen G2 beta-barrel {430-667} MOTIF: cysteine residue {C618} MODIFICATION: cysteine residue {C411} EGF domain {668-709} MOTIF: cysteine residue {C672} MODIFICATION: cysteine residue {C685} cysteine residue {C679} MODIFICATION: cysteine residue {C695} cysteine residue {C685} MODIFICATION: cysteine residue {C672} cysteine residue {C695} MODIFICATION: cysteine residue {C679} cysteine residue {C697} MODIFICATION: cysteine residue {C708} Cell attachment site {702-704} cysteine residue {C708} MODIFICATION: cysteine residue {C697} EGF domain {710-751} MOTIF: cysteine residue {C714} MODIFICATION: cysteine residue {C727} cysteine residue {C721} MODIFICATION: cysteine residue {C736} cysteine residue {C727} MODIFICATION: cysteine residue {C714} cysteine residue {C736} MODIFICATION: cysteine residue {C721} cysteine residue {C738} MODIFICATION: cysteine residue {C750} cysteine residue {C750} MODIFICATION: cysteine residue {C738} EGF domain {758-801} MOTIF: cysteine residue {C762} MODIFICATION: cysteine residue {C777} cysteine residue {C769} MODIFICATION: cysteine residue {C787} cysteine residue {C777} MODIFICATION: cysteine residue {C762} cysteine residue {C787} MODIFICATION: cysteine residue {C769} cysteine residue {C789} MODIFICATION: cysteine residue {C800} cysteine residue {C800} MODIFICATION: cysteine residue {C789} EGF domain {802-840} MOTIF: cysteine residue {C806} MODIFICATION: cysteine residue {C817} cysteine residue {C811} MODIFICATION: cysteine residue {C826} cysteine residue {C817} MODIFICATION: cysteine residue {C806} cysteine residue {C826} MODIFICATION: cysteine residue {C811} cysteine residue {C828} MODIFICATION: cysteine residue {C839} cysteine residue {C839} MODIFICATION: cysteine residue {C828} Thyroglobulin type-1 {846-919} MOTIF: cysteine residue {C849} MODIFICATION: cysteine residue {C878} cysteine residue {C878} MODIFICATION: cysteine residue {C849} cysteine residue {C889} MODIFICATION: cysteine residue {C896} cysteine residue {C896} MODIFICATION: cysteine residue {C889} cysteine residue {C898} MODIFICATION: cysteine residue {C919} cysteine residue {C919} MODIFICATION: cysteine residue {C898} LDL-receptor class B {990-1032} LDL-receptor class B {1033-1075} LDL-receptor class B {1076-1120} LDL-receptor class B {1121-1162} MOTIF: N-glycosylation site {N1137} EGF domain {1208-1244} MOTIF: cysteine residue {C1212} MODIFICATION: cysteine residue {C1223} cysteine residue {C1219} MODIFICATION: cysteine residue {C1232} cysteine residue {C1223} MODIFICATION: cysteine residue {C1212} cysteine residue {C1232} MODIFICATION: cysteine residue {C1219} cysteine residue {C1234} MODIFICATION: cysteine residue {C1243} cysteine residue {C1243} MODIFICATION: cysteine residue {C1234}

Database Correlations

OMIM 131390 UniProt P14543 PFAM correlations Entrez Gene 4811 Kegg hsa:4811

References

  1. UniProt :accession P14543
  2. Mann et al EMBO J 8:65 1989 (mouse sequence)
  3. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 920