NID2_MOUSE
ID NID2_MOUSE Reviewed; 1403 AA.
AC O88322; Q7TQF0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Nidogen-2;
DE Short=NID-2;
DE AltName: Full=Entactin-2;
DE Flags: Precursor;
GN Name=Nid2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9633511; DOI=10.1006/excr.1998.4016;
RA Kimura N., Toyoshima T., Kojima T., Shimane M.;
RT "Entactin-2: a new member of basement membrane protein with high homology
RT to entactin/nidogen.";
RL Exp. Cell Res. 241:36-45(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP INTERACTION WITH LAMA2.
RX PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan
RT to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
RT proteins.";
RL EMBO J. 18:863-870(1999).
RN [5]
RP INTERACTION WITH EFEMP2.
RX PubMed=17324935; DOI=10.1074/jbc.m611029200;
RA Kobayashi N., Kostka G., Garbe J.H., Keene D.R., Baechinger H.P.,
RA Hanisch F.G., Markova D., Tsuda T., Timpl R., Chu M.L., Sasaki T.;
RT "A comparative analysis of the fibulin protein family. Biochemical
RT characterization, binding interactions, and tissue localization.";
RL J. Biol. Chem. 282:11805-11816(2007).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-681.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1336, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Cell adhesion glycoprotein. Might be involved in osteoblast
CC differentiation. It probably has a role in cell-extracellular matrix
CC interactions.
CC -!- SUBUNIT: Interacts with LAMA2. Interacts with COL13A1 (By similarity).
CC Interacts with EFEMP2 (PubMed:17324935). {ECO:0000250,
CC ECO:0000269|PubMed:17324935}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- PTM: Highly N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; AB017202; BAA32609.1; -; mRNA.
DR EMBL; CH466613; EDL01537.1; -; Genomic_DNA.
DR EMBL; BC054746; AAH54746.1; -; mRNA.
DR EMBL; BC057016; AAH57016.1; -; mRNA.
DR CCDS; CCDS36813.1; -.
DR RefSeq; NP_032721.2; NM_008695.2.
DR AlphaFoldDB; O88322; -.
DR SMR; O88322; -.
DR BioGRID; 201771; 11.
DR STRING; 10090.ENSMUSP00000022340; -.
DR GlyGen; O88322; 4 sites.
DR iPTMnet; O88322; -.
DR PhosphoSitePlus; O88322; -.
DR jPOST; O88322; -.
DR MaxQB; O88322; -.
DR PaxDb; O88322; -.
DR PeptideAtlas; O88322; -.
DR PRIDE; O88322; -.
DR ProteomicsDB; 252965; -.
DR Antibodypedia; 10737; 174 antibodies from 30 providers.
DR DNASU; 18074; -.
DR Ensembl; ENSMUST00000022340; ENSMUSP00000022340; ENSMUSG00000021806.
DR GeneID; 18074; -.
DR KEGG; mmu:18074; -.
DR UCSC; uc007siu.1; mouse.
DR CTD; 22795; -.
DR MGI; MGI:1298229; Nid2.
DR VEuPathDB; HostDB:ENSMUSG00000021806; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000157901; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR InParanoid; O88322; -.
DR OMA; VYPYCPA; -.
DR OrthoDB; 95286at2759; -.
DR PhylomeDB; O88322; -.
DR TreeFam; TF320666; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR BioGRID-ORCS; 18074; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Nid2; mouse.
DR PRO; PR:O88322; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O88322; protein.
DR Bgee; ENSMUSG00000021806; Expressed in humerus cartilage element and 231 other tissues.
DR ExpressionAtlas; O88322; baseline and differential.
DR Genevisible; O88322; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
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; 5.
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 1: Evidence at protein level;
KW Basement membrane; Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Methylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1403
FT /note="Nidogen-2"
FT /id="PRO_0000007672"
FT DOMAIN 108..274
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 507..547
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 551..781
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 782..823
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 824..862
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 871..914
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 915..953
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 965..1033
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1044..1112
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1182..1225
FT /note="LDL-receptor class B 1"
FT REPEAT 1226..1268
FT /note="LDL-receptor class B 2"
FT REPEAT 1269..1313
FT /note="LDL-receptor class B 3"
FT REPEAT 1314..1355
FT /note="LDL-receptor class B 4"
FT REPEAT 1357..1401
FT /note="LDL-receptor class B 5"
FT REGION 323..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 946..948
FT /note="Cell attachment site"
FT COMPBIAS 1024..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1336
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 511..524
FT /evidence="ECO:0000250"
FT DISULFID 518..533
FT /evidence="ECO:0000250"
FT DISULFID 535..546
FT /evidence="ECO:0000250"
FT DISULFID 786..799
FT /evidence="ECO:0000250"
FT DISULFID 793..809
FT /evidence="ECO:0000250"
FT DISULFID 811..822
FT /evidence="ECO:0000250"
FT DISULFID 828..841
FT /evidence="ECO:0000250"
FT DISULFID 835..850
FT /evidence="ECO:0000250"
FT DISULFID 852..865
FT /evidence="ECO:0000250"
FT DISULFID 875..890
FT /evidence="ECO:0000250"
FT DISULFID 882..900
FT /evidence="ECO:0000250"
FT DISULFID 902..913
FT /evidence="ECO:0000250"
FT DISULFID 919..930
FT /evidence="ECO:0000250"
FT DISULFID 924..939
FT /evidence="ECO:0000250"
FT DISULFID 941..952
FT /evidence="ECO:0000250"
FT DISULFID 968..991
FT /evidence="ECO:0000250"
FT DISULFID 1002..1009
FT /evidence="ECO:0000250"
FT DISULFID 1011..1033
FT /evidence="ECO:0000250"
FT DISULFID 1047..1071
FT /evidence="ECO:0000250"
FT DISULFID 1082..1089
FT /evidence="ECO:0000250"
FT DISULFID 1091..1112
FT /evidence="ECO:0000250"
FT CONFLICT 197
FT /note="L -> F (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> F (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> V (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="P -> H (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="S -> W (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="S -> F (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="R -> C (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="L -> F (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="L -> F (in Ref. 1; BAA32609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 153913 MW; ABA0B1DB2C84A27A CRC64;
MFRDPTAGWL TPPSPLSLLV MLLLLSRVGA LRPDELFPYG ESWGDQLLPE GDDESSAAVK
LAIPLRFYDA QFSSLYVGTN GIISTQDFPR ETQYVDDDFP TDFPAIAPFL ADIDTSHSRG
RILYREDTSG AVLSLAARYV RTGFPLSGSS FTPTHAFLAT WEHVGAYEEV SRGAAPSGEL
NTFQAVLASD ESDTYALFLY PANGLQFFGT RPKESYNVQL QLPARVGFCR GEADDLKREA
LYFSLTNTEQ SVKNLYQLSN LGIPGVWAFH IGSRFALDNV RPATVGGDPS TARSSALEHP
FSHAAALESY TEDSFHYYDE NEEDVEYPPV EPGEAPEGHS RIDVSFNSKA DPGLVDVGTS
SPGSDRASPW PYPAPGNWPS YRETESASLD PQTKQGRPVG EGEVLDFRDP AELLDQMGTR
APAPPEADAA LLTPVNEDLG GRNTQSYPEA GPVPSEPDVP VPPLEGEVLP HYPESGHVPP
LRGGKYVIGL EDHVGSNDQV FTYNGANLET CEHSHGRCSQ HAFCTDYTTG FCCHCQSRFY
GNGKHCLPEG APHRVNGKVS GRLRVGHIPV HFTDVDLHAY IVGNDGRAYT AISHVPQPAA
QALLPVLPIG GLFGWLFALE KPGSENGFSL TGATFVHDVE VTFHPGEERV RITQTAEGLD
PENYLSIKTN IEGQVPFIPA NFTAHITPYK EFYHYRDSVV TSSSSRSFSL TSGSINQTWS
YHIDQNITYQ ACRHAPRHLA IPATQQLTVD RAFALYSEDE GVLRFAVTNQ IGPVEVDSAP
VGVNPCYDGS HTCDTTARCH PGTGVDYTCE CTPGFQGDGR SCVDVNECAT GFHRCGPNSV
CVNLVGSYRC ECRSGYEFAD DQHTCILIAP PPNPCLDGSH TCAPEGQARC IHHGGSSFSC
ACLPGFIGTG HQCSDVDECA ENRCHEAAIC YNTPGSFSCR CQPGYRGDGF HCTSDTVPED
SISGLKPCEY QQRYAQTQHA YPGSRIHIPQ CDDQGNFVPL QCHGSTGFCW CVDRNGHEVP
GTQTPPGSTP PHCGPPPEPT QRPRTVCERW RESLLEHYGG TPRDDQYVPQ CDDLGHFIPL
QCHGKSDFCW CVDKDGRELQ GTRSQPGTRP ACIPTVAPPV VRPTPRPDVT PPSVGTFLLY
AQGQQIGHLP LNGSRLQKDA ARTLLSLHGS IVVGIDYDCR ERMVYWTDVA GRTISRASLE
AGAEPETIIT SGLISPEGLA IDHFRRTMYW TDSGLDKIER AELDGSERKV LFHTDLVNPR
AITVDPIRGN LYWTDWNREA PKIETSSLDG ENRRILINKD IGLPNGLTFD PFSKLLCWAD
AGTKKLECTL PDGTGRRVIQ NHLNYPFSIV SYADHFYHTD WRRDGVISVN KDSGQFTDEF
LPEQRSHLYG ITAVYPYCPT GRK
