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P10493

- NID1_MOUSE

UniProt

P10493 - NID1_MOUSE

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Protein

Nidogen-1

Gene

Nid1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei457 – 4571Involved in perlecan binding
Sitei459 – 4591Involved in perlecan binding
Sitei648 – 6481Involved in perlecan binding

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. collagen binding Source: MGI
  3. extracellular matrix binding Source: MGI
  4. laminin-1 binding Source: MGI

GO - Biological processi

  1. cell-matrix adhesion Source: MGI
  2. extracellular matrix organization Source: MGI
  3. glomerular basement membrane development Source: MGI
  4. positive regulation of cell-substrate adhesion Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

Protein family/group databases

MEROPSiI63.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Nidogen-1
Short name:
NID-1
Alternative name(s):
Entactin
Gene namesi
Name:Nid1
Synonyms:Ent
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:97342. Nid1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: MGI
  3. cell periphery Source: MGI
  4. extracellular matrix Source: UniProtKB
  5. extracellular region Source: Reactome
  6. extracellular vesicular exosome Source: Ensembl
  7. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 12451217Nidogen-1PRO_0000007670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi187 – 1871N-linked (GlcNAc...)1 Publication
Modified residuei290 – 2901SulfotyrosineSequence Analysis
Modified residuei295 – 2951SulfotyrosineSequence Analysis
Glycosylationi299 – 2991O-linked (GalNAc...)1 Publication
Glycosylationi331 – 3311O-linked (GalNAc...)1 Publication
Glycosylationi337 – 3371O-linked (GalNAc...)1 Publication
Glycosylationi345 – 3451O-linked (GalNAc...)1 Publication
Glycosylationi348 – 3481O-linked (GalNAc...); partial1 Publication
Disulfide bondi388 ↔ 401
Disulfide bondi395 ↔ 410
Disulfide bondi409 ↔ 616
Disulfide bondi412 ↔ 423
Glycosylationi415 – 4151N-linked (GlcNAc...)1 Publication
Disulfide bondi670 ↔ 683By similarity
Disulfide bondi677 ↔ 693By similarity
Disulfide bondi695 ↔ 706By similarity
Disulfide bondi712 ↔ 725By similarity
Disulfide bondi719 ↔ 734By similarity
Disulfide bondi736 ↔ 748By similarity
Disulfide bondi760 ↔ 775By similarity
Disulfide bondi767 ↔ 785By similarity
Disulfide bondi787 ↔ 798By similarity
Disulfide bondi804 ↔ 815By similarity
Disulfide bondi809 ↔ 824By similarity
Disulfide bondi826 ↔ 837By similarity
Disulfide bondi847 ↔ 876By similarity
Disulfide bondi887 ↔ 894By similarity
Disulfide bondi896 ↔ 917By similarity
Glycosylationi920 – 9201O-linked (GalNAc...)1 Publication
Glycosylationi933 – 9331O-linked (GalNAc...)1 Publication
Disulfide bondi1210 ↔ 1221By similarity
Disulfide bondi1217 ↔ 1230By similarity
Disulfide bondi1232 ↔ 1241By similarity

Post-translational modificationi

N- and O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

MaxQBiP10493.
PaxDbiP10493.
PRIDEiP10493.

PTM databases

PhosphoSiteiP10493.

Miscellaneous databases

PMAP-CutDBP10493.

Expressioni

Gene expression databases

BgeeiP10493.
CleanExiMM_NID1.
ExpressionAtlasiP10493. baseline and differential.
GenevestigatoriP10493.

Interactioni

Subunit structurei

Interacts with FBLN1 and LGALS3BP. Interacts with PLXDC1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamc1P024683EBI-1032117,EBI-7059830

Protein-protein interaction databases

BioGridi201770. 4 interactions.
IntActiP10493. 3 interactions.
MINTiMINT-215381.

Structurei

Secondary structure

1
1245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi388 – 3914
Helixi392 – 3943
Beta strandi399 – 4035
Beta strandi408 – 4125
Beta strandi416 – 4183
Beta strandi420 – 4256
Beta strandi429 – 44214
Beta strandi449 – 46113
Turni462 – 4643
Beta strandi466 – 4738
Helixi476 – 4794
Helixi480 – 4823
Helixi487 – 4959
Helixi506 – 5105
Beta strandi513 – 52210
Beta strandi525 – 5273
Beta strandi529 – 5368
Beta strandi547 – 5548
Beta strandi562 – 5643
Beta strandi568 – 5758
Beta strandi578 – 59013
Beta strandi601 – 61212
Beta strandi627 – 64115
Turni642 – 6454
Beta strandi646 – 65611
Beta strandi942 – 96019
Helixi964 – 9663
Beta strandi968 – 98417
Turni985 – 9884
Beta strandi989 – 9946
Turni995 – 9984
Beta strandi999 – 10079
Beta strandi1011 – 10144
Beta strandi1021 – 10277
Turni1028 – 10314
Beta strandi1032 – 10376
Turni1038 – 10414
Beta strandi1042 – 10476
Beta strandi1054 – 10574
Beta strandi1062 – 10709
Turni1071 – 10744
Beta strandi1075 – 10806
Beta strandi1083 – 10853
Beta strandi1087 – 10926
Beta strandi1099 – 11024
Beta strandi1109 – 11157
Turni1116 – 11194
Beta strandi1120 – 11256
Turni1126 – 11294
Beta strandi1130 – 11356
Beta strandi1138 – 11469
Beta strandi1150 – 11578
Beta strandi1160 – 11656
Turni1166 – 11694
Beta strandi1170 – 11756
Turni1176 – 11794
Beta strandi1180 – 11856
Beta strandi1196 – 11994

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GL4X-ray2.00A385-665[»]
1H4UX-ray2.20A395-659[»]
1NPEX-ray2.30A941-1207[»]
ProteinModelPortaliP10493.
SMRiP10493. Positions 387-659, 666-909, 940-1233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10493.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 268163NIDOPROSITE-ProRule annotationAdd
BLAST
Domaini384 – 42441EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini428 – 665238Nidogen G2 beta-barrelPROSITE-ProRule annotationAdd
BLAST
Domaini666 – 70742EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini708 – 74942EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini756 – 79944EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini800 – 83839EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini844 – 91774Thyroglobulin type-1PROSITE-ProRule annotationAdd
BLAST
Repeati988 – 103043LDL-receptor class B 1Add
BLAST
Repeati1031 – 107343LDL-receptor class B 2Add
BLAST
Repeati1074 – 111845LDL-receptor class B 3Add
BLAST
Repeati1119 – 116042LDL-receptor class B 4Add
BLAST
Domaini1206 – 124237EGF-like 6PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi700 – 7023Cell attachment site

Sequence similaritiesi

Contains 6 EGF-like domains.PROSITE-ProRule annotation
Contains 4 LDL-receptor class B repeats.PROSITE-ProRule annotation
Contains 1 NIDO domain.PROSITE-ProRule annotation
Contains 1 nidogen G2 beta-barrel domain.PROSITE-ProRule annotation
Contains 1 thyroglobulin type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG282695.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000072712.
HOVERGENiHBG006498.
InParanoidiP10493.
KOiK06826.
OMAiDYRPDYR.
OrthoDBiEOG7M0NQN.
TreeFamiTF320666.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.40.155.10. 2 hits.
4.10.800.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000033. LDLR_classB_rpt.
IPR003886. Nidogen_extracell_dom.
IPR000716. Thyroglobulin_1.
[Graphical view]
PfamiPF12662. 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]
SMARTiSM00181. 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]
SUPFAMiSSF54511. SSF54511. 1 hit.
SSF57184. SSF57184. 2 hits.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10493-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLDASGCSWA MWTWALLQLL LLVGPGGCLN RQELFPFGPG QGDLELEAGD
60 70 80 90 100
DVVSPSLELI GELSFYDRTD ITSVYVTTNG IIAMSEPPAT EYHPGTFPPS
110 120 130 140 150
FGSVAPFLAD LDTTDGLGNV YYREDLSPFI IQMAAEYVQR GFPEVSFQPT
160 170 180 190 200
SVVVVTWESV APYGGPSSSP AEEGKRNTFQ AVLASSNSSS YAIFLYPEDG
210 220 230 240 250
LQFFTTFSKK DESQVPAVVG FSKGLVGFLW KSNGAYNIFA NDRESIENLA
260 270 280 290 300
KSSNAGHQGV WVFEIGSPAT AKGVVSADVN LDLDDDGADY EDEDYDLVTS
310 320 330 340 350
HLGLEDVATP SPSHSPRRGY PDPHNVPRIL SPGYEATERP RGVPTERTRS
360 370 380 390 400
FQLPAERFPQ HHPQVIDVDE VEETGVVFSY NTGSQQTCAN NRHQCSVHAE
410 420 430 440 450
CRDYATGFCC RCVANYTGNG RQCVAEGSPQ RVNGKVKGRI FVGSSQVPVV
460 470 480 490 500
FENTDLHSYV VMNHGRSYTA ISTIPETVGY SLLPLAPIGG IIGWMFAVEQ
510 520 530 540 550
DGFKNGFSIT GGEFTRQAEV TFLGHPGKLV LKQQFSGIDE HGHLTISTEL
560 570 580 590 600
EGRVPQIPYG ASVHIEPYTE LYHYSSSVIT SSSTREYTVM EPDQDGAAPS
610 620 630 640 650
HTHIYQWRQT ITFQECAHDD ARPALPSTQQ LSVDSVFVLY NKEERILRYA
660 670 680 690 700
LSNSIGPVRD GSPDALQNPC YIGTHGCDSN AACRPGPGTQ FTCECSIGFR
710 720 730 740 750
GDGQTCYDID ECSEQPSRCG NHAVCNNLPG TFRCECVEGY HFSDRGTCVA
760 770 780 790 800
AEDQRPINYC ETGLHNCDIP QRAQCIYMGG SSYTCSCLPG FSGDGRACRD
810 820 830 840 850
VDECQHSRCH PDAFCYNTPG SFTCQCKPGY QGDGFRCMPG EVSKTRCQLE
860 870 880 890 900
REHILGAAGG ADAQRPTLQG MFVPQCDEYG HYVPTQCHHS TGYCWCVDRD
910 920 930 940 950
GRELEGSRTP PGMRPPCLST VAPPIHQGPV VPTAVIPLPP GTHLLFAQTG
960 970 980 990 1000
KIERLPLERN TMKKTEAKAF LHIPAKVIIG LAFDCVDKVV YWTDISEPSI
1010 1020 1030 1040 1050
GRASLHGGEP TTIIRQDLGS PEGIALDHLG RTIFWTDSQL DRIEVAKMDG
1060 1070 1080 1090 1100
TQRRVLFDTG LVNPRGIVTD PVRGNLYWTD WNRDNPKIET SHMDGTNRRI
1110 1120 1130 1140 1150
LAQDNLGLPN GLTFDAFSSQ LCWVDAGTHR AECLNPAQPG RRKVLEGLQY
1160 1170 1180 1190 1200
PFAVTSYGKN LYYTDWKTNS VIAMDLAISK EMDTFHPHKQ TRLYGITIAL
1210 1220 1230 1240
SQCPQGHNYC SVNNGGCTHL CLPTPGSRTC RCPDNTLGVD CIERK
Length:1,245
Mass (Da):136,538
Last modified:July 27, 2011 - v2
Checksum:i92D12D128E6EF144
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701P → L in CAA32642. (PubMed:2496973)Curated
Sequence conflicti659 – 6591R → K in CAA32642. (PubMed:2496973)Curated
Sequence conflicti967 – 9671A → R in CAA32408. (PubMed:3264556)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26244.1.
PIRiS02730. MMMSND.
RefSeqiNP_035047.2. NM_010917.2.
UniGeneiMm.4691.

Genome annotation databases

EnsembliENSMUST00000005532; ENSMUSP00000005532; ENSMUSG00000005397.
GeneIDi18073.
KEGGimmu:18073.
UCSCiuc007pmf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26244.1.
PIRi S02730. MMMSND.
RefSeqi NP_035047.2. NM_010917.2.
UniGenei Mm.4691.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P10493.
SMRi P10493. Positions 387-659, 666-909, 940-1233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201770. 4 interactions.
IntActi P10493. 3 interactions.
MINTi MINT-215381.

Protein family/group databases

MEROPSi I63.001.

PTM databases

PhosphoSitei P10493.

Proteomic databases

MaxQBi P10493.
PaxDbi P10493.
PRIDEi P10493.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005532 ; ENSMUSP00000005532 ; ENSMUSG00000005397 .
GeneIDi 18073.
KEGGi mmu:18073.
UCSCi uc007pmf.2. mouse.

Organism-specific databases

CTDi 4811.
MGIi MGI:97342. Nid1.

Phylogenomic databases

eggNOGi NOG282695.
GeneTreei ENSGT00760000118968.
HOGENOMi HOG000072712.
HOVERGENi HBG006498.
InParanoidi P10493.
KOi K06826.
OMAi DYRPDYR.
OrthoDBi EOG7M0NQN.
TreeFami TF320666.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.

Miscellaneous databases

ChiTaRSi NID1. mouse.
EvolutionaryTracei P10493.
NextBioi 293199.
PMAP-CutDB P10493.
PROi P10493.
SOURCEi Search...

Gene expression databases

Bgeei P10493.
CleanExi MM_NID1.
ExpressionAtlasi P10493. baseline and differential.
Genevestigatori P10493.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
2.40.155.10. 2 hits.
4.10.800.10. 1 hit.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000033. LDLR_classB_rpt.
IPR003886. Nidogen_extracell_dom.
IPR000716. Thyroglobulin_1.
[Graphical view ]
Pfami PF12662. 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 ]
SMARTi 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 ]
SUPFAMi SSF54511. SSF54511. 1 hit.
SSF57184. SSF57184. 2 hits.
SSF57610. SSF57610. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiNID1_MOUSE
AccessioniPrimary (citable) accession number: P10493
Secondary accession number(s): Q3TKX9
, Q8BQI3, Q8C3U8, Q8C9P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3