NID2_RAT
ID NID2_RAT Reviewed; 1396 AA.
AC B5DFC9; Q5M812;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nidogen-2;
DE Short=NID-2;
DE Flags: Precursor;
GN Name=Nid2;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Cell adhesion glycoprotein. Might be involved in osteoblast
CC differentiation. It probably has a role in cell-extracellular matrix
CC interactions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LAMA2. Interacts with COL13A1 (By similarity).
CC Interacts with EFEMP2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O88322}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B5DFC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B5DFC9-2; Sequence=VSP_038781;
CC -!- PTM: Highly N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; CH474061; EDL86201.1; -; Genomic_DNA.
DR EMBL; BC088325; AAH88325.1; -; mRNA.
DR EMBL; BC169012; AAI69012.1; -; mRNA.
DR RefSeq; NP_001012005.2; NM_001012005.2. [B5DFC9-1]
DR AlphaFoldDB; B5DFC9; -.
DR SMR; B5DFC9; -.
DR STRING; 10116.ENSRNOP00000000383; -.
DR GlyGen; B5DFC9; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; B5DFC9; -.
DR PhosphoSitePlus; B5DFC9; -.
DR PaxDb; B5DFC9; -.
DR PeptideAtlas; B5DFC9; -.
DR PRIDE; B5DFC9; -.
DR Ensembl; ENSRNOT00000000383; ENSRNOP00000000383; ENSRNOG00000000341. [B5DFC9-1]
DR Ensembl; ENSRNOT00000082196; ENSRNOP00000072586; ENSRNOG00000000341. [B5DFC9-2]
DR GeneID; 302248; -.
DR KEGG; rno:302248; -.
DR UCSC; RGD:1311685; rat. [B5DFC9-1]
DR CTD; 22795; -.
DR RGD; 1311685; Nid2.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000157901; -.
DR InParanoid; B5DFC9; -.
DR OrthoDB; 95286at2759; -.
DR PhylomeDB; B5DFC9; -.
DR TreeFam; TF320666; -.
DR Reactome; R-RNO-3000157; Laminin interactions.
DR PRO; PR:B5DFC9; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 2.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 4.10.800.10; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 4.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 4.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Methylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1396
FT /note="Nidogen-2"
FT /id="PRO_0000392064"
FT DOMAIN 108..274
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 500..540
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 544..774
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 775..816
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 817..859
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 864..907
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 908..944
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 958..1026
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1037..1105
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1175..1218
FT /note="LDL-receptor class B 1"
FT REPEAT 1219..1261
FT /note="LDL-receptor class B 2"
FT REPEAT 1262..1306
FT /note="LDL-receptor class B 3"
FT REPEAT 1307..1348
FT /note="LDL-receptor class B 4"
FT REGION 346..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1329
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88322"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 504..517
FT /evidence="ECO:0000250"
FT DISULFID 511..526
FT /evidence="ECO:0000250"
FT DISULFID 528..539
FT /evidence="ECO:0000250"
FT DISULFID 779..792
FT /evidence="ECO:0000250"
FT DISULFID 786..802
FT /evidence="ECO:0000250"
FT DISULFID 804..815
FT /evidence="ECO:0000250"
FT DISULFID 821..834
FT /evidence="ECO:0000250"
FT DISULFID 828..843
FT /evidence="ECO:0000250"
FT DISULFID 845..858
FT /evidence="ECO:0000250"
FT DISULFID 868..883
FT /evidence="ECO:0000250"
FT DISULFID 875..893
FT /evidence="ECO:0000250"
FT DISULFID 895..906
FT /evidence="ECO:0000250"
FT DISULFID 912..923
FT /evidence="ECO:0000250"
FT DISULFID 917..932
FT /evidence="ECO:0000250"
FT DISULFID 961..984
FT /evidence="ECO:0000250"
FT DISULFID 995..1002
FT /evidence="ECO:0000250"
FT DISULFID 1004..1026
FT /evidence="ECO:0000250"
FT DISULFID 1040..1064
FT /evidence="ECO:0000250"
FT DISULFID 1075..1082
FT /evidence="ECO:0000250"
FT DISULFID 1084..1105
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038781"
SQ SEQUENCE 1396 AA; 152976 MW; C0C9D1C6943240D7 CRC64;
MSWDPTAGRL APPSPLSLLL VLVLLSRVGA LRPEELFPYG ESWGDRLLPE GDDESSAAVK
LAVPLRFYDA QFSNLYVGTN GIISTQDFPR ETQYVDDDFP TDFPAIAPFL ADIDTSHSRG
RILYREDTSQ AVLSLAARYV RTGFPLTGSS FTPTHAFLAT WEHVGAYEEV RRGAAPSGEL
NTFQAVLASD ESDTYALFLY PANGLQFFGT RPKESYNVQL QLPARVGFCR GEADDLKREA
LYFSLTNTEQ SVKNLYQLSN LGIPGAWAFH IGSRLALDNV RPATVGGDHS TARSSALEHS
FNHAAALESY TEDSFDYYNE NEEDVEYPPI EPGEALEGHS RIDVSFNSEV NPTSPDSDHA
SPLPHPAPGN WPSYRETESA SLDPQTKQGP PVGEVEVLDF KDPAELLDQT GTRTPAPPGA
DAAFLTPGRE DLGNRDTQSY PEARPVPSEP DVPVAPLERE ILPNYPESGH VPPLSGGRYV
VGLEDHVSSK DQVFTYNGAN RETCEHSHGQ CSRHAFCTDY TTGFCCHCQS RFYGNGRHCV
PEGAPHRVNG KVSGHLQVGH MPVHFTDVDL HAYIVSNDGR AYTAISQIPQ PAAQALLPVL
PIGGLFGWLF ALEKPGSENG FSLTGATFVH DVEVTFHPGE ERVRITQTAE GLDPENYLSL
NTNIEGQVPF IPANFTAHIA PYQEFYHHRD SVVTSSSSRS FSLISGSINQ TRSYRIDQNI
TYKACSHAPR HLAVPATQQL TVDRAFALYS EEEGVLRFAV TNQIGPVEVD SAPTAVNPCY
DGSHTCDTTA RCHPGTGVDY TCECTPGFQG DGRSCVDVNE CATGFHRCGP NSVCVNLVGS
YRCECRSGYE FADDRHTCVL IAPPPNPCLD GSHTCAPEGQ ARCIHHGGSS FSCACLPGFV
GTGHQCSDVD ECAENRCHGA AICYNTPGSF SCRCQPGYHG DGFHCASDTV PEDSISGLKP
CEYQQRYAQA QHAHAGSRIH IPQCDDQGNF VPLQCHGSTG FCWCVDQNGH EVPGTQTPPG
STPPHCGPPP EPTQRPRTVC ERWRESLLEH YGGTPRDDQY VPQCDDLGHF IPLQCHGKSD
FCWCVDKDGR ELPGTRSQPG TMPACIPTVA PPVVRPTPRP DVTPPAVGTF LLYAQGQQIG
HLPLNGSRLQ KDAARTLLSL HGSIVVGIDY DCRERMVYWT DVAGRTISRA SLEAGAEPET
IITSGLISPE GLAIDHFRRT MYWTDSGLDK IERAGLDGSE RKVLFHTDLV NPRAITVDPI
RGNLYWTDWN REAPKIETSS LDGENRRILI NKDIGLPNGL TFDPFSKLLC WADAGTKKLE
CTLPDGTGRR VIQNHLNYPF SVVSYADHFY HTDWRRDGVI SVSKDSGQLT DEYLPEQRSH
LYGITAVYPY CPTGRK
