ID   NID1_RAT                Reviewed;         324 AA.
AC   P08460; Q712L9;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Nidogen-1;
DE            Short=NID-1;
DE   AltName: Full=Entactin;
DE   Flags: Fragment;
GN   Name=Nid1; Synonyms=Nid;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3264556; DOI=10.1083/jcb.107.6.2749;
RA   Durkin M.E., Chakravarti S., Bartos B.B., Liu S.H., Friedman R.L.,
RA   Chung A.E.;
RT   "Amino acid sequence and domain structure of entactin. Homology with
RT   epidermal growth factor precursor and low density lipoprotein receptor.";
RL   J. Cell Biol. 107:2749-2756(1988).
RN   [2]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3470744; DOI=10.1073/pnas.84.6.1570;
RA   Durkin M.E., Carlin B.E., Vergnes J., Bartos B.B., Merlie J., Chung A.E.;
RT   "Carboxyl-terminal sequence of entactin deduced from a cDNA clone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:1570-1574(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 211-319.
RC   STRAIN=Wistar;
RX   PubMed=10727019; DOI=10.1078/s0171-9335(04)70013-8;
RA   Konrad L., Albrecht M., Renneberg H., Ulrix W., Hoeben E., Verhoeven G.,
RA   Aumuller G.;
RT   "Mesenchymal entactin-1 (nidogen-1) is required for adhesion of peritubular
RT   cells of the rat testis in vitro.";
RL   Eur. J. Cell Biol. 79:112-120(2000).
CC   -!- FUNCTION: Sulfated glycoprotein widely distributed in basement
CC       membranes and tightly associated with laminin. Also binds to collagen
CC       IV and perlecan. It probably has a role in cell-extracellular matrix
CC       interactions.
CC   -!- SUBUNIT: Interacts with FBLN1 and LGALS3BP. Interacts with PLXDC1 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P08460; Q91ZV7: Plxdc1; Xeno; NbExp=2; IntAct=EBI-8280787, EBI-8280807;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- PTM: N- and O-glycosylated.
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DR   EMBL; M15797; AAA41120.1; ALT_SEQ; mRNA.
DR   EMBL; AJ224450; CAA11963.1; -; mRNA.
DR   PIR; S14828; S14828.
DR   AlphaFoldDB; P08460; -.
DR   SMR; P08460; -.
DR   IntAct; P08460; 2.
DR   MINT; P08460; -.
DR   STRING; 10116.ENSRNOP00000003349; -.
DR   GlyGen; P08460; 1 site.
DR   PaxDb; P08460; -.
DR   PeptideAtlas; P08460; -.
DR   PRIDE; P08460; -.
DR   UCSC; RGD:3178; rat.
DR   RGD; 3178; Nid1.
DR   eggNOG; KOG1214; Eukaryota.
DR   InParanoid; P08460; -.
DR   PhylomeDB; P08460; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005604; C:basement membrane; ISO:RGD.
DR   GO; GO:0071944; C:cell periphery; ISO:RGD.
DR   GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005518; F:collagen binding; ISO:RGD.
DR   GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR   GO; GO:0043236; F:laminin binding; ISO:RGD.
DR   GO; GO:0043237; F:laminin-1 binding; ISO:RGD.
DR   GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR   GO; GO:0032836; P:glomerular basement membrane development; ISO:RGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR   InterPro; IPR003886; NIDO_dom.
DR   Pfam; PF06119; NIDO; 1.
DR   SMART; SM00539; NIDO; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS51220; NIDO; 1.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Secreted;
KW   Sulfation.
FT   CHAIN           <1..>324
FT                   /note="Nidogen-1"
FT                   /id="PRO_0000055634"
FT   DOMAIN          16..178
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          295..>324
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          219..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         205
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        299..312
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        306..321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT   NON_TER         324
SQ   SEQUENCE   324 AA;  35661 MW;  CBDEAD3337019027 CRC64;
     EFHPGTFPPS FGSVAPFLAD LDTTDGLGNV YYREDLSPFI IQMAAEYVQR GFPEVSFQPT
     SVVVVTWESM APYGGPSGSL VEEGKRNTFQ AVLASSNSSS YAIFLYPDDG LQFFTTFSKK
     DENQVPAVVG FSKGLEGFLW KSNGAYNIFA NDRESIENLA KSSNAGHQGV WVFEIGSPAT
     AKGVVPADVN LDVDDDGADY EDEDYDLQTS HLGLEDVATQ PFPSHSPRRG YPDPHNVPRT
     LAPSYEATER PHGIPTERTK SFQLPVERFP QKHPQVIDVD EVEETGVVFS YNTGSQQTCA
     NNRHQCSVHA ECRDYATGFC CRCV