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P10493 (NID1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

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. Interacts with PLXDC1. Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Post-translational modification

N- and O-glycosylated. Ref.8

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1
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...) Ref.8
Glycosylation2991O-linked (GalNAc...) Ref.8
Glycosylation3311O-linked (GalNAc...) Ref.8
Glycosylation3371O-linked (GalNAc...) Ref.8
Glycosylation3451O-linked (GalNAc...) Ref.8
Glycosylation3481O-linked (GalNAc...); partial Ref.8
Glycosylation4151N-linked (GlcNAc...) Ref.8
Glycosylation9201O-linked (GalNAc...) Ref.8
Glycosylation9331O-linked (GalNAc...) Ref.8
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 conflict9671A → R in CAA32408. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P10493 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 92D12D128E6EF144

FASTA1,245136,538
        10         20         30         40         50         60 
MLDASGCSWA MWTWALLQLL LLVGPGGCLN RQELFPFGPG QGDLELEAGD DVVSPSLELI 

        70         80         90        100        110        120 
GELSFYDRTD ITSVYVTTNG IIAMSEPPAT EYHPGTFPPS FGSVAPFLAD LDTTDGLGNV 

       130        140        150        160        170        180 
YYREDLSPFI IQMAAEYVQR GFPEVSFQPT SVVVVTWESV APYGGPSSSP AEEGKRNTFQ 

       190        200        210        220        230        240 
AVLASSNSSS YAIFLYPEDG LQFFTTFSKK DESQVPAVVG FSKGLVGFLW KSNGAYNIFA 

       250        260        270        280        290        300 
NDRESIENLA KSSNAGHQGV WVFEIGSPAT AKGVVSADVN LDLDDDGADY EDEDYDLVTS 

       310        320        330        340        350        360 
HLGLEDVATP SPSHSPRRGY PDPHNVPRIL SPGYEATERP RGVPTERTRS FQLPAERFPQ 

       370        380        390        400        410        420 
HHPQVIDVDE VEETGVVFSY NTGSQQTCAN NRHQCSVHAE CRDYATGFCC RCVANYTGNG 

       430        440        450        460        470        480 
RQCVAEGSPQ RVNGKVKGRI FVGSSQVPVV FENTDLHSYV VMNHGRSYTA ISTIPETVGY 

       490        500        510        520        530        540 
SLLPLAPIGG IIGWMFAVEQ DGFKNGFSIT GGEFTRQAEV TFLGHPGKLV LKQQFSGIDE 

       550        560        570        580        590        600 
HGHLTISTEL EGRVPQIPYG ASVHIEPYTE LYHYSSSVIT SSSTREYTVM EPDQDGAAPS 

       610        620        630        640        650        660 
HTHIYQWRQT ITFQECAHDD ARPALPSTQQ LSVDSVFVLY NKEERILRYA LSNSIGPVRD 

       670        680        690        700        710        720 
GSPDALQNPC YIGTHGCDSN AACRPGPGTQ FTCECSIGFR GDGQTCYDID ECSEQPSRCG 

       730        740        750        760        770        780 
NHAVCNNLPG TFRCECVEGY HFSDRGTCVA AEDQRPINYC ETGLHNCDIP QRAQCIYMGG 

       790        800        810        820        830        840 
SSYTCSCLPG FSGDGRACRD VDECQHSRCH PDAFCYNTPG SFTCQCKPGY QGDGFRCMPG 

       850        860        870        880        890        900 
EVSKTRCQLE REHILGAAGG ADAQRPTLQG MFVPQCDEYG HYVPTQCHHS TGYCWCVDRD 

       910        920        930        940        950        960 
GRELEGSRTP PGMRPPCLST VAPPIHQGPV VPTAVIPLPP GTHLLFAQTG KIERLPLERN 

       970        980        990       1000       1010       1020 
TMKKTEAKAF LHIPAKVIIG LAFDCVDKVV YWTDISEPSI GRASLHGGEP TTIIRQDLGS 

      1030       1040       1050       1060       1070       1080 
PEGIALDHLG RTIFWTDSQL DRIEVAKMDG TQRRVLFDTG LVNPRGIVTD PVRGNLYWTD 

      1090       1100       1110       1120       1130       1140 
WNRDNPKIET SHMDGTNRRI LAQDNLGLPN GLTFDAFSSQ LCWVDAGTHR AECLNPAQPG 

      1150       1160       1170       1180       1190       1200 
RRKVLEGLQY PFAVTSYGKN LYYTDWKTNS VIAMDLAISK EMDTFHPHKQ TRLYGITIAL 

      1210       1220       1230       1240 
SQCPQGHNYC SVNNGGCTHL CLPTPGSRTC RCPDNTLGVD CIERK

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor."
Durkin M.E., Chakravarti S., Bartos B.B., Liu S.H., Friedman R.L., Chung A.E.
J. Cell Biol. 107:2749-2756(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40.
[2]"Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells."
Mann K., Deutzmann R., Aumailley M., Timpl R., Raimondi L., Yamamda Y., Pan T.-C., Conway D., Chu M.-L.
EMBO J. 8:65-72(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic lung and Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Characterization of the 5' end of the mouse Ent gene encoding the basement membrane protein, entactin."
Durkin M.E., Liu S.H., Reing J., Chung A.E.
Gene 132:261-266(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
Strain: BALB/c.
Tissue: Liver.
[6]"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."
Durkin M.E., Wewer U.M., Chung A.E.
Genomics 26:219-228(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1207-1245.
Strain: C57BL/6J X CBA/J.
[7]"Purification and structural characterization of intact and fragmented nidogen obtained from a tumor basement membrane."
Paulsson M., Deutzmann R., Dziadek M., Nowack H., Timpl R., Weber S., Engel J.
Eur. J. Biochem. 156:467-478(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[8]"Structure and localization of O- and N-linked oligosaccharide chains on basement membrane protein nidogen."
Fujiwara S., Shinkai H., Mann K., Timpl R.
Matrix 13:215-222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-187; THR-299; SER-331; THR-337; THR-345; THR-348; ASN-415; THR-920 AND THR-933, PARTIAL PROTEIN SEQUENCE.
[9]"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."
Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.
J. Mol. Biol. 272:226-236(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1.
[10]"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."
Sasaki T., Brakebusch C., Engel J., Timpl R.
EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LGALS3BP.
[11]"Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies."
Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.
Eur. J. Biochem. 268:5119-5128(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1.
[12]"Identification of the basement membrane protein nidogen as a candidate ligand for tumor endothelial marker 7 in vitro and in vivo."
Lee H.K., Seo I.A., Park H.K., Park H.T.
FEBS Lett. 580:2253-2257(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXDC1.
[13]"Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1."
Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.
Nat. Struct. Biol. 8:634-640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-665.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X14194 mRNA. Translation: CAA32408.1.
X14480 mRNA. Translation: CAA32642.1.
AK041633 mRNA. Translation: BAC31014.1.
AK084876 mRNA. Translation: BAC39300.1.
AK144878 mRNA. Translation: BAE26114.1.
AK166779 mRNA. Translation: BAE39014.1.
BC131669 mRNA. Translation: AAI31670.1.
AH003206 Genomic DNA. Translation: AAA77652.1.
X83093 Genomic DNA. Translation: CAA58148.1.
IPIIPI00111793.
PIRMMMSND. S02730.
RefSeqNP_035047.2. NM_010917.2.
UniGeneMm.4691.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GL4X-ray2.00A385-665[»]
1H4UX-ray2.20A395-659[»]
1NPEX-ray2.30A941-1207[»]
ProteinModelPortalP10493.
SMRP10493. Positions 387-659, 666-1244.
ModBaseSearch...

Protein-protein interaction databases

IntActP10493. 1 interaction.
MINTMINT-215381.

PTM databases

PhosphoSiteP10493.

Proteomic databases

PaxDbP10493.
PRIDEP10493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005532; ENSMUSP00000005532; ENSMUSG00000005397.
GeneID18073.
KEGGmmu:18073.

Organism-specific databases

CTD4811.
MGIMGI:97342. Nid1.

Phylogenomic databases

eggNOGNOG282695.
GeneTreeENSGT00690000101695.
HOGENOMHOG000072712.
HOVERGENHBG006498.
InParanoidQ3TKX9.
KOK06826.
OMADYRPDYR.
OrthoDBEOG4BCDM4.

Gene expression databases

ArrayExpressP10493.
BgeeP10493.
CleanExMM_NID1.
GenevestigatorP10493.
GermOnlineENSMUSG00000005397. Mus musculus.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
2.40.155.10. 2 hits.
4.10.800.10. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR006605. G2_nidogen/fibulin_G2F.
IPR009017. GFP.
IPR023413. GFP_like.
IPR000033. LDLR_classB_rpt.
IPR003886. Nidogen_extracell_dom.
IPR000716. Thyroglobulin_1.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 1 hit.
PF07474. G2F. 1 hit.
PF00058. Ldl_recept_b. 3 hits.
PF06119. NIDO. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
SM00682. G2F. 1 hit.
SM00135. LY. 5 hits.
SM00539. NIDO. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMSSF54511. GFP_like. 1 hit.
SSF57610. Thyroglobulin_1. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 2 hits.
PS51120. LDLRB. 4 hits.
PS51220. NIDO. 1 hit.
PS50993. NIDOGEN_G2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNID1. mouse.
EvolutionaryTraceP10493.
NextBio293199.
PMAP-CutDBP10493.
SOURCESearch...

Entry information

Entry nameNID1_MOUSE
AccessionPrimary (citable) accession number: P10493
Secondary accession number(s): Q3TKX9 expand/collapse secondary AC list , Q8BQI3, Q8C3U8, Q8C9P6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents