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UniProtKB/Swiss-Prot entry P10493


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NID1_MOUSE
Primary accession number P10493
Secondary accession numbers Q8BQI3 Q8C3U8 Q8C9P6
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 101)
Name and origin of the protein
Protein name Nidogen-1 [Precursor]
Synonym Entactin
Gene name
Name: Nid1
Synonyms: Ent
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-40.
DOI=10.1083/jcb.107.6.2749; PubMed=3264556 [NCBI, ExPASy, EBI, Israel, Japan]
Durkin M.E., Chakravarti S., Bartos B.B., Liu S.H., Friedman R.L., Chung A.E.;
"Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.";
J. Cell Biol. 107:2749-2756(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2496973 [NCBI, ExPASy, EBI, Israel, Japan]
Mann K., Deutzmann R., Aumailley M., Timpl R., Raimondi L., Yamamda Y., Pan T.-C., Conway D., Chu M.-L.;
"Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells.";
EMBO J. 8:65-72(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryonic lung, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1016/0378-1119(93)90205-H; PubMed=8224873 [NCBI, ExPASy, EBI, Israel, Japan]
Durkin M.E., Liu S.H., Reing J., Chung A.E.;
"Characterization of the 5' end of the mouse Ent gene encoding the basement membrane protein, entactin.";
Gene 132:261-266(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1207-1245.
STRAIN=C57BL/6J X CBA/J;
DOI=10.1016/0888-7543(95)80204-Y; PubMed=7601446 [NCBI, ExPASy, EBI, Israel, Japan]
Durkin M.E., Wewer U.M., Chung A.E.;
"Exon organization of the mouse entactin gene corresponds to the structural domains of the polypeptide and has regional homology to the low-density lipoprotein receptor gene.";
Genomics 26:219-228(1995).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=3084254 [NCBI, ExPASy, EBI, Israel, Japan]
Paulsson M., Deutzmann R., Dziadek M., Nowack H., Timpl R., Weber S., Engel J.;
"Purification and structural characterization of intact and fragmented nidogen obtained from a tumor basement membrane.";
Eur. J. Biochem. 156:467-478(1986).
[7]
GLYCOSYLATION AT ASN-187; THR-299; SER-331; THR-337; THR-345; THR-348; ASN-415; THR-920 AND THR-933, AND PARTIAL PROTEIN SEQUENCE.
PubMed=8326911 [NCBI, ExPASy, EBI, Israel, Japan]
Fujiwara S., Shinkai H., Mann K., Timpl R.;
"Structure and localization of O- and N-linked oligosaccharide chains on basement membrane protein nidogen.";
Matrix 13:215-222(1993).
[8]
INTERACTION WITH FBLN1.
DOI=10.1006/jmbi.1997.1244; PubMed=9299350 [NCBI, ExPASy, EBI, Israel, Japan]
Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
"Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules.";
J. Mol. Biol. 272:226-236(1997).
[9]
INTERACTION WITH LGALS3BP.
DOI=10.1093/emboj/17.6.1606; PubMed=9501082 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki T., Brakebusch C., Engel J., Timpl R.;
"Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin.";
EMBO J. 17:1606-1613(1998).
[10]
INTERACTION WITH FBLN1.
PubMed=11589703 [NCBI, ExPASy, EBI, Israel, Japan]
Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
"Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies.";
Eur. J. Biochem. 268:5119-5128(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-665.
DOI=10.1038/89683; PubMed=11427896 [NCBI, ExPASy, EBI, Israel, Japan]
Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.;
"Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.";
Nat. Struct. Biol. 8:634-640(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X14194; CAA32408.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14480; CAA32642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK041633; BAC31014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK084876; BAC39300.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17324; AAA77652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17322; AAA77652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17323; AAA77652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83093; CAA58148.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02730; MMMSND.
UniGene Mm.4691
3D structure databases
PDB
1GL4; X-ray; 2.00 A; A=385-665.[ExPASy / RCSB / EBI]
1H4U; X-ray; 2.20 A; A=395-659.[ExPASy / RCSB / EBI]
1NPE; X-ray; 2.30 A; A=941-1207.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GL4; -.
1H4U; -.
1NPE; -.
ModBase P10493.
Protein-protein interaction databases
IntAct P10493; -.
Organism-specific databases
MGI MGI:97342; Nid1.
Gene expression databases
ArrayExpress P10493; -.
CleanEx MM_NID1; -.
GermOnline ENSMUSG00000005397; Mus musculus.
Ontologies
GO
GO:0005604; Cellular component: basement membrane (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007160; Biological process: cell-matrix adhesion (inferred from direct assay from MGI).
GO:0032836; Biological process: glomerular basement membrane development (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR011042; 6-blade_b-propeller_TolB-like.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR006605; G2F.
IPR000033; LDLR.
IPR003886; NIDO.
IPR000716; Thyroglobulin_1.
Graphical view of domain structure.
Gene3D G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
G3DSA:4.10.800.10; Thyroglobulin_1; 1.
Pfam PF00008; EGF; 3.
PF07645; EGF_CA; 2.
PF07474; G2F; 1.
PF00058; Ldl_recept_b; 3.
PF06119; NIDO; 1.
PF00086; Thyroglobulin_1; 1.
Pfam graphical view of domain structure.
SMART SM00181; EGF; 4.
SM00179; EGF_CA; 2.
SM00682; G2F; 1.
SM00135; LY; 5.
SM00539; NIDO; 1.
SM00211; TY; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 3.
PS00022; EGF_1; 1.
PS01186; EGF_2; 4.
PS50026; EGF_3; 5.
PS01187; EGF_CA; 2.
PS51120; LDLRB; 4.
PS51220; NIDO; 1.
PS50993; NIDOGEN_G2; 1.
PS00484; THYROGLOBULIN_1_1; 1.
PS51162; THYROGLOBULIN_1_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P10493.
Genome annotation databases
Ensembl ENSMUSG00000005397; Mus musculus. [Contig view]
KEGG mmu:18073; -.
Phylogenomic databases
HOGENOM P10493; -.
HOVERGEN P10493; -.
Other
SOURCE Nid1; Mus musculus.
ProtoNet P10493.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Basement membrane; Calcium; Cell adhesion; Direct protein sequencing; EGF-like domain; Extracellular matrix; Glycoprotein; Repeat; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     28  28      
CHAIN   29   1245  1217     Nidogen-1. PRO_0000007670
DOMAIN   106    268  163     NIDO. 
DOMAIN   384    424  41     EGF-like 1. 
DOMAIN   428    665  238     Nidogen G2 beta-barrel. 
DOMAIN   666    707  42     EGF-like 2. 
DOMAIN   708    749  42     EGF-like 3; calcium-binding (Potential). 
DOMAIN   756    799  44     EGF-like 4. 
DOMAIN   800    838  39     EGF-like 5; calcium-binding (Potential). 
DOMAIN   844    917  74     Thyroglobulin type-1. 
REPEAT   988   1030  43     LDL-receptor class B 1. 
REPEAT   1031   1073  43     LDL-receptor class B 2. 
REPEAT   1074   1118  45     LDL-receptor class B 3. 
REPEAT   1119   1160  42     LDL-receptor class B 4. 
DOMAIN   1206   1242  37     EGF-like 6. 
MOTIF   700    702  3     Cell attachment site. 
SITE   457    457  1     Involved in perlecan binding. 
SITE   459    459  1     Involved in perlecan binding. 
SITE   648    648  1     Involved in perlecan binding. 
MOD_RES   290    290        Sulfotyrosine (Potential). 
MOD_RES   295    295        Sulfotyrosine (Potential). 
CARBOHYD   187    187        N-linked (GlcNAc...). 
CARBOHYD   299    299        O-linked (GalNAc...). 
CARBOHYD   331    331        O-linked (GalNAc...). 
CARBOHYD   337    337        O-linked (GalNAc...). 
CARBOHYD   345    345        O-linked (GalNAc...). 
CARBOHYD   348    348        O-linked (GalNAc...); partial. 
CARBOHYD   415    415        N-linked (GlcNAc...). 
CARBOHYD   920    920        O-linked (GalNAc...). 
CARBOHYD   933    933        O-linked (GalNAc...). 
DISULFID   388    401         
DISULFID   395    410         
DISULFID   409    616         
DISULFID   412    423         
DISULFID   670    683        By similarity. 
DISULFID   677    693        By similarity. 
DISULFID   695    706        By similarity. 
DISULFID   712    725        By similarity. 
DISULFID   719    734        By similarity. 
DISULFID   736    748        By similarity. 
DISULFID   760    775        By similarity. 
DISULFID   767    785        By similarity. 
DISULFID   787    798        By similarity. 
DISULFID   804    815        By similarity. 
DISULFID   809    824        By similarity. 
DISULFID   826    837        By similarity. 
DISULFID   847    876        By similarity. 
DISULFID   887    894        By similarity. 
DISULFID   896    917        By similarity. 
DISULFID   1210   1221        By similarity. 
DISULFID   1217   1230        By similarity. 
DISULFID   1232   1241        By similarity. 
CONFLICT   170    170        P -> L (in Ref. 2; CAA32642). 
CONFLICT   659    659        R -> K (in Ref. 2; CAA32642). 
CONFLICT   967    967        R -> A (in Ref. 2; CAA32642/BAC39300). 
HELIX   388    391  4      
HELIX   392    394  3      
STRAND   399    403  5      
STRAND   408    412  5      
STRAND   416    418  3      
STRAND   420    425  6      
STRAND   429    442  14      
STRAND   449    461  13      
TURN   462    464  3      
STRAND   466    473  8      
HELIX   476    479  4      
HELIX   480    482  3      
HELIX   487    495  9      
HELIX   506    510  5      
STRAND   513    522  10      
STRAND   525    527  3      
STRAND   529    536  8      
STRAND   547    554  8      
STRAND   562    564  3      
STRAND   568    575  8      
STRAND   578    590  13      
STRAND   601    612  12      
STRAND   627    641  15      
TURN   642    645  4      
STRAND   646    656  11      
STRAND   942    960  19      
HELIX   964    966  3      
STRAND   968    984  17      
TURN   985    988  4      
STRAND   989    994  6      
TURN   995    998  4      
STRAND   999   1007  9