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Reviewed, UniProtKB/Swiss-Prot P10493 (NID1_MOUSE)

Last modified November 25, 2008. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Nidogen-1
      Short name=NID-1
Alternative name(s):
    Entactin
Gene names
Name: Nid1
Synonyms: Ent
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions.

Subunit structure

Interacts with FBLN1 and LGALS3BP.

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Post-translational modification

N- and O-glycosylated.

Sequence similarities

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.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hspg2Q057931EBI-1032117,EBI-1032089

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 12451217Nidogen-1
PRO_0000007670

Regions

Domain106 – 268163NIDO
Domain384 – 42441EGF-like 1
Domain428 – 665238Nidogen G2 beta-barrel
Domain666 – 70742EGF-like 2
Domain708 – 74942EGF-like 3; calcium-binding Potential
Domain756 – 79944EGF-like 4
Domain800 – 83839EGF-like 5; calcium-binding Potential
Domain844 – 91774Thyroglobulin type-1
Repeat988 – 103043LDL-receptor class B 1
Repeat1031 – 107343LDL-receptor class B 2
Repeat1074 – 111845LDL-receptor class B 3
Repeat1119 – 116042LDL-receptor class B 4
Domain1206 – 124237EGF-like 6
Motif700 – 7023Cell attachment site

Sites

Site4571Involved in perlecan binding
Site4591Involved in perlecan binding
Site6481Involved in perlecan binding

Amino acid modifications

Modified residue2901Sulfotyrosine Potential
Modified residue2951Sulfotyrosine Potential
Glycosylation1871N-linked (GlcNAc...)
Glycosylation2991O-linked (GalNAc...)
Glycosylation3311O-linked (GalNAc...)
Glycosylation3371O-linked (GalNAc...)
Glycosylation3451O-linked (GalNAc...)
Glycosylation3481O-linked (GalNAc...); partial
Glycosylation4151N-linked (GlcNAc...)
Glycosylation9201O-linked (GalNAc...)
Glycosylation9331O-linked (GalNAc...)
Disulfide bond388 ↔ 401
Disulfide bond395 ↔ 410
Disulfide bond409 ↔ 616
Disulfide bond412 ↔ 423
Disulfide bond670 ↔ 683 By similarity
Disulfide bond677 ↔ 693 By similarity
Disulfide bond695 ↔ 706 By similarity
Disulfide bond712 ↔ 725 By similarity
Disulfide bond719 ↔ 734 By similarity
Disulfide bond736 ↔ 748 By similarity
Disulfide bond760 ↔ 775 By similarity
Disulfide bond767 ↔ 785 By similarity
Disulfide bond787 ↔ 798 By similarity
Disulfide bond804 ↔ 815 By similarity
Disulfide bond809 ↔ 824 By similarity
Disulfide bond826 ↔ 837 By similarity
Disulfide bond847 ↔ 876 By similarity
Disulfide bond887 ↔ 894 By similarity
Disulfide bond896 ↔ 917 By similarity
Disulfide bond1210 ↔ 1221 By similarity
Disulfide bond1217 ↔ 1230 By similarity
Disulfide bond1232 ↔ 1241 By similarity

Experimental info

Sequence conflict1701P → L in CAA32642. Ref.2
Sequence conflict6591R → K in CAA32642. Ref.2
Sequence conflict9671R → A in CAA32642 and BAC39300. Ref.2

Secondary structure

1 .............................................................................................. 1245
Helix Strand Turn

Details...