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P10493

- NID1_MOUSE

UniProt

P10493 - NID1_MOUSE

Protein

Nidogen-1

Gene

Nid1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    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

    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, 666-833, 845-909, 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.
    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

    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, 666-833, 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

    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 1, 2014
    This is version 159 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