Reviewed, UniProtKB/Swiss-Prot P10493 (NID1_MOUSE)

Names and origin

Protein names

Recommended name:
    Nidogen-1
      Short name=NID-1
Alternative name(s):
    Entactin

Gene names

Name:	Nid1
Synonyms:	Ent

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1245 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.8 Ref.9 Ref.10
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
Post-translational modification	N- and O-glycosylated. Ref.7
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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
PTM	Disulfide bond Glycoprotein Sulfation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	bioluminescence Inferred from electronic annotation. Source: InterPro cell-matrix adhesion Inferred from direct assay. Source: MGI glomerular basement membrane development Inferred from direct assay. Source: MGI positive regulation of cell-substrate adhesion Inferred from direct assay. Source: MGI protein-chromophore linkage Inferred from electronic annotation. Source: InterPro
Cellular component	basement membrane Inferred from direct assay. Source: MGI extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix binding Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hspg2	Q05793	1	EBI-1032117,EBI-1032089

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.1

Chain

29 – 1245

1217

Nidogen-1

PRO_0000007670

Regions

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

Sites

Site

457

1

Involved in perlecan binding

Site

459

1

Involved in perlecan binding

Site

648

1

Involved in perlecan binding

Amino acid modifications

Modified residue

290

1

Sulfotyrosine Potential

Modified residue

295

1

Sulfotyrosine Potential

Glycosylation

187

1

N-linked (GlcNAc...) Ref.7

Glycosylation

299

1

O-linked (GalNAc...) Ref.7

Glycosylation

331

1

O-linked (GalNAc...) Ref.7

Glycosylation

337

1

O-linked (GalNAc...) Ref.7

Glycosylation

345

1

O-linked (GalNAc...) Ref.7

Glycosylation

348

1

O-linked (GalNAc...); partial Ref.7

Glycosylation

415

1

N-linked (GlcNAc...) Ref.7

Glycosylation

920

1

O-linked (GalNAc...) Ref.7

Glycosylation

933

1

O-linked (GalNAc...) Ref.7

Disulfide bond

388 ↔ 401

Disulfide bond

395 ↔ 410

Disulfide bond

409 ↔ 616

Disulfide bond

412 ↔ 423

Disulfide bond

670 ↔ 683

By similarity

Disulfide bond

677 ↔ 693

By similarity

Disulfide bond

695 ↔ 706

By similarity

Disulfide bond

712 ↔ 725

By similarity

Disulfide bond

719 ↔ 734

By similarity

Disulfide bond

736 ↔ 748

By similarity

Disulfide bond

760 ↔ 775

By similarity

Disulfide bond

767 ↔ 785

By similarity

Disulfide bond

787 ↔ 798

By similarity

Disulfide bond

804 ↔ 815

By similarity

Disulfide bond

809 ↔ 824

By similarity

Disulfide bond

826 ↔ 837

By similarity

Disulfide bond

847 ↔ 876

By similarity

Disulfide bond

887 ↔ 894

By similarity

Disulfide bond

896 ↔ 917

By similarity

Disulfide bond

1210 ↔ 1221

By similarity

Disulfide bond

1217 ↔ 1230

By similarity

Disulfide bond

1232 ↔ 1241

By similarity

Experimental info

Sequence conflict

170

1

P → L in CAA32642. Ref.2

Sequence conflict

659

1

R → K in CAA32642. Ref.2

Sequence conflict

967

1

R → A in CAA32642. Ref.2

Sequence conflict

967

1

R → A in BAC39300. Ref.2

Secondary structure

1

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1245

Helix Strand Turn

Details...

Helix

388 – 391

4

Helix

392 – 394

3

Beta strand

399 – 403

5

Beta strand

408 – 412

5

Beta strand

416 – 418

3

Beta strand

420 – 425

6

Beta strand

429 – 442

14

Beta strand

449 – 461

13

Turn

462 – 464

3

Beta strand

466 – 473

8

Helix

476 – 479

4

Helix

480 – 482

3

Helix

487 – 495

9

Helix

506 – 510

5

Beta strand

513 – 522

10

Beta strand

525 – 527

3

Beta strand

529 – 536

8

Beta strand

547 – 554

8

Beta strand

562 – 564

3

Beta strand

568 – 575

8

Beta strand

578 – 590

13

Beta strand

601 – 612

12

Beta strand

627 – 641

15

Turn

642 – 645

4

Beta strand

646 – 656

11

Beta strand

942 – 960

19

Helix

964 – 966

3

Beta strand

968 – 984

17

Turn

985 – 988

4

Beta strand

989 – 994

6

Turn

995 – 998

4

Beta strand

999 – 1007

9

Beta strand

1011 – 1014

4

Beta strand

1021 – 1027

7

Turn

1028 – 1031

4

Beta strand

1032 – 1037

6

Turn

1038 – 1041

4

Beta strand

1042 – 1047

6

Beta strand

1054 – 1057

4

Beta strand

1062 – 1070

9

Turn

1071 – 1074

4

Beta strand

1075 – 1080

6

Beta strand

1083 – 1085

3

Beta strand

1087 – 1092

6

Beta strand

1099 – 1102

4

Beta strand

1109 – 1115

7

Turn

1116 – 1119

4

Beta strand

1120 – 1125

6

Turn

1126 – 1129

4

Beta strand

1130 – 1135

6

Beta strand

1138 – 1146

9

Beta strand

1150 – 1157

8

Beta strand

1160 – 1165

6

Turn

1166 – 1169

4

Beta strand

1170 – 1175

6

Turn

1176 – 1179

4

Beta strand

1180 – 1185

6

Beta strand

1196 – 1199

4

Sequences

	Sequence		Length	Mass (Da)
	P10493-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 8FBE276F29BEF6D2	FASTA	1,245	136,623
	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 TMKKTERKAF 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

References

	« Hide 'large scale' referencesShow '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: 3264556] [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: 2496973] [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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic lung and Thymus.
[4]	"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: 8224873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251. Strain: BALB/c. Tissue: Liver.
[5]	"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: 7601446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1207-1245. Strain: C57BL/6J X CBA/J.
[6]	"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: 3084254] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[7]	"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: 8326911] [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.
[8]	"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: 9299350] [Abstract] Cited for: INTERACTION WITH FBLN1.
[9]	"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: 9501082] [Abstract] Cited for: INTERACTION WITH LGALS3BP.
[10]	"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: 11589703] [Abstract] Cited for: INTERACTION WITH FBLN1.
[11]	"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: 11427896] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-665.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X14194 mRNA. Translation: CAA32408.1.
X14480 mRNA. Translation: CAA32642.1.
AK041633 mRNA. Translation: BAC31014.1.
AK084876 mRNA. Translation: BAC39300.1.
L17324, L17322, L17323 Genomic DNA. Translation: AAA77652.1.
X83093 Genomic DNA. Translation: CAA58148.1.

IPI

IPI00111793.

PIR

MMMSND. S02730.

UniGene

Mm.4691

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GL4	X-ray	2.00	A	385-665	[»]
1H4U	X-ray	2.20	A	395-659	[»]
1NPE	X-ray	2.30	A	941-1207	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P10493. 1 interaction.

Proteomic databases

PRIDE

P10493.

Genome annotation databases

Ensembl

ENSMUSG00000005397. Mus musculus. [Contig view]

Organism-specific databases

MGI

MGI:97342. Nid1.

Phylogenomic databases

HOGENOM

P10493.

HOVERGEN

P10493.

Gene expression databases

ArrayExpress

P10493.

Bgee

P10493.

CleanEx

MM_NID1.

GermOnline

ENSMUSG00000005397. Mus musculus.

Family and domain databases

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR006605. G2F.
IPR000033. LDLR.
IPR003886. NIDO.
IPR000716. Thyroglobulin_1.
[Graphical view]

Gene3D

G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
G3DSA:4.10.800.10. Thyroglobulin_1. 1 hit.

Pfam

PF00008. EGF. 2 hits.
PF07645. EGF_CA. 2 hits.
PF07474. G2F. 1 hit.
PF00058. Ldl_recept_b. 3 hits.
PF06119. NIDO. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]

SMART

SM00181. 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]

PROSITE

PS00010. 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]

ProtoNet

Search...

Other Resources

PMAP-CutDB

P10493.

SOURCE

Search...

Entry information

Entry name

NID1_MOUSE

Accession

Primary (citable) accession number: P10493
Secondary accession number(s): Q8BQI3, Q8C3U8, Q8C9P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)