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P10493

- NID1_MOUSE

UniProt

P10493 - NID1_MOUSE

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Protein
Nidogen-1
Gene
Nid1, Ent
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
  5. protein 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 region Source: Reactome
  5. 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 Publication
Add
BLAST
Chaini29 – 12451217Nidogen-1
PRO_0000007670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi187 – 1871N-linked (GlcNAc...)1 Publication
Modified residuei290 – 2901Sulfotyrosine Reviewed prediction
Modified residuei295 – 2951Sulfotyrosine Reviewed prediction
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 ↔ 683 By similarity
Disulfide bondi677 ↔ 693 By similarity
Disulfide bondi695 ↔ 706 By similarity
Disulfide bondi712 ↔ 725 By similarity
Disulfide bondi719 ↔ 734 By similarity
Disulfide bondi736 ↔ 748 By similarity
Disulfide bondi760 ↔ 775 By similarity
Disulfide bondi767 ↔ 785 By similarity
Disulfide bondi787 ↔ 798 By similarity
Disulfide bondi804 ↔ 815 By similarity
Disulfide bondi809 ↔ 824 By similarity
Disulfide bondi826 ↔ 837 By similarity
Disulfide bondi847 ↔ 876 By similarity
Disulfide bondi887 ↔ 894 By similarity
Disulfide bondi896 ↔ 917 By similarity
Glycosylationi920 – 9201O-linked (GalNAc...)1 Publication
Glycosylationi933 – 9331O-linked (GalNAc...)1 Publication
Disulfide bondi1210 ↔ 1221 By similarity
Disulfide bondi1217 ↔ 1230 By similarity
Disulfide bondi1232 ↔ 1241 By 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

ArrayExpressiP10493.
BgeeiP10493.
CleanExiMM_NID1.
GenevestigatoriP10493.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi201770. 4 interactions.
IntActiP10493. 2 interactions.
MINTiMINT-215381.

Structurei

Secondary structure

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, 666-833, 845-909, 940-1233.

Miscellaneous databases

EvolutionaryTraceiP10493.

Family & Domainsi

Domains and Repeats

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

Motif

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

Sequence similaritiesi

Contains 6 EGF-like domains.
Contains 1 NIDO domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG282695.
GeneTreeiENSGT00750000117524.
HOGENOMiHOG000072712.
HOVERGENiHBG006498.
InParanoidiQ3TKX9.
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

MLDASGCSWA MWTWALLQLL LLVGPGGCLN RQELFPFGPG QGDLELEAGD     50
DVVSPSLELI GELSFYDRTD ITSVYVTTNG IIAMSEPPAT EYHPGTFPPS 100
FGSVAPFLAD LDTTDGLGNV YYREDLSPFI IQMAAEYVQR GFPEVSFQPT 150
SVVVVTWESV APYGGPSSSP AEEGKRNTFQ AVLASSNSSS YAIFLYPEDG 200
LQFFTTFSKK DESQVPAVVG FSKGLVGFLW KSNGAYNIFA NDRESIENLA 250
KSSNAGHQGV WVFEIGSPAT AKGVVSADVN LDLDDDGADY EDEDYDLVTS 300
HLGLEDVATP SPSHSPRRGY PDPHNVPRIL SPGYEATERP RGVPTERTRS 350
FQLPAERFPQ HHPQVIDVDE VEETGVVFSY NTGSQQTCAN NRHQCSVHAE 400
CRDYATGFCC RCVANYTGNG RQCVAEGSPQ RVNGKVKGRI FVGSSQVPVV 450
FENTDLHSYV VMNHGRSYTA ISTIPETVGY SLLPLAPIGG IIGWMFAVEQ 500
DGFKNGFSIT GGEFTRQAEV TFLGHPGKLV LKQQFSGIDE HGHLTISTEL 550
EGRVPQIPYG ASVHIEPYTE LYHYSSSVIT SSSTREYTVM EPDQDGAAPS 600
HTHIYQWRQT ITFQECAHDD ARPALPSTQQ LSVDSVFVLY NKEERILRYA 650
LSNSIGPVRD GSPDALQNPC YIGTHGCDSN AACRPGPGTQ FTCECSIGFR 700
GDGQTCYDID ECSEQPSRCG NHAVCNNLPG TFRCECVEGY HFSDRGTCVA 750
AEDQRPINYC ETGLHNCDIP QRAQCIYMGG SSYTCSCLPG FSGDGRACRD 800
VDECQHSRCH PDAFCYNTPG SFTCQCKPGY QGDGFRCMPG EVSKTRCQLE 850
REHILGAAGG ADAQRPTLQG MFVPQCDEYG HYVPTQCHHS TGYCWCVDRD 900
GRELEGSRTP PGMRPPCLST VAPPIHQGPV VPTAVIPLPP GTHLLFAQTG 950
KIERLPLERN TMKKTEAKAF LHIPAKVIIG LAFDCVDKVV YWTDISEPSI 1000
GRASLHGGEP TTIIRQDLGS PEGIALDHLG RTIFWTDSQL DRIEVAKMDG 1050
TQRRVLFDTG LVNPRGIVTD PVRGNLYWTD WNRDNPKIET SHMDGTNRRI 1100
LAQDNLGLPN GLTFDAFSSQ LCWVDAGTHR AECLNPAQPG RRKVLEGLQY 1150
PFAVTSYGKN LYYTDWKTNS VIAMDLAISK EMDTFHPHKQ TRLYGITIAL 1200
SQCPQGHNYC SVNNGGCTHL CLPTPGSRTC RCPDNTLGVD CIERK 1245
Length:1,245
Mass (Da):136,538
Last modified:July 27, 2011 - v2
Checksum:i92D12D128E6EF144
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701P → L in CAA32642. 1 Publication
Sequence conflicti659 – 6591R → K in CAA32642. 1 Publication
Sequence conflicti967 – 9671A → R in CAA32408. 1 Publication

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, 666-833, 845-909, 940-1233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201770. 4 interactions.
IntActi P10493. 2 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 ENSGT00750000117524.
HOGENOMi HOG000072712.
HOVERGENi HBG006498.
InParanoidi Q3TKX9.
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

ArrayExpressi P10493.
Bgeei P10493.
CleanExi MM_NID1.
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: September 3, 2014
This is version 158 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

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