ID A6QNS6_BOVIN Unreviewed; 1241 AA.
AC A6QNS6; F1MWN3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=NID1 protein {ECO:0000313|EMBL:AAI48975.1};
DE SubName: Full=Nidogen 1 {ECO:0000313|Ensembl:ENSBTAP00000009531.6};
GN Name=NID1 {ECO:0000313|EMBL:AAI48975.1,
GN ECO:0000313|Ensembl:ENSBTAP00000009531.6,
GN ECO:0000313|VGNC:VGNC:55991};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI48975.1};
RN [1] {ECO:0000313|EMBL:AAI48975.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI48975.1};
RC TISSUE=Fetal muscle {ECO:0000313|EMBL:AAI48975.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000009531.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009531.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000009531.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009531.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; BC148974; AAI48975.1; -; mRNA.
DR RefSeq; NP_001094625.1; NM_001101155.1.
DR STRING; 9913.ENSBTAP00000009531; -.
DR Ensembl; ENSBTAT00000009531.6; ENSBTAP00000009531.6; ENSBTAG00000007244.6.
DR GeneID; 534319; -.
DR KEGG; bta:534319; -.
DR CTD; 4811; -.
DR VEuPathDB; HostDB:ENSBTAG00000007244; -.
DR VGNC; VGNC:55991; NID1.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000156318; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR OMA; PGTGNQF; -.
DR OrthoDB; 25347at2759; -.
DR TreeFam; TF320666; -.
DR Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000007244; Expressed in omental fat pad and 102 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0043237; F:laminin-1 binding; IEA:Ensembl.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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 PANTHER; PTHR46513:SF6; NIDOGEN-1; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 3.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 5.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF54511; GFP-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 2: Evidence at transcript level;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1241
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041198226"
FT DOMAIN 106..268
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 427..664
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 665..706
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 707..745
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 755..798
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 799..835
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 843..913
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 984..1026
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1027..1069
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1070..1114
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 309..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 883..890
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1241 AA; 136001 MW; A9657FD189967B56 CRC64;
MLATVRRSGA AWTRALLLQL LLAGPGGCLS RQELFPFGPE HGDLELEAGD DLVSPALELS
TALHFFDRSD IDSVYVTTNG IIAMSEPPAK ETHPGPFPPT FGAVAPFLAD LDTTDGLGKV
YYREDLSPSV TQLAAECVQR GFPEVSFKPS SAVVVTWESV APYQGPSKDP TLEGKRNTFQ
SILASSDSST YAIFLYPEDG LQFYTTFSKK EENQVPAVVA FSQGLVGLIW KSDGAYNIFA
NDKESIGNLA KSSNSGLQGI WVFEIGSPAT ASGVVPADVN LGLDDGTEYD DEDYDSVTRV
GLEDAVTTSF PYEAPGRGDS GTYNTPSDLS PRRMATERPL TPPTEKTRSF QLPGERFPQQ
QPQVIDVDEV EETEIVFRYN TDSRQTCANN RHQCSVHAEC RDFATGFCCR CVAGYTGNGR
QCVAEGSPQR VNGKVKGRIF VGDSQVPIVF ENTDLHSYVV MNHGRSYTAI STIPETVGYS
LLPLAPIGGI IGWMFAVEQD GFKNGFSITG GEFTRQAEVT FVGHRDKLII KQQFSGIDEH
GHLTIDTELE GRVPQIAFGS SVHIEPYTEL YHYSRQVITS FSTREYTVTE PERHGTAPSH
AHTYRWRQTI TFRECLHDDS RPALPSTQQL SVDSVFVLYN QEERILRYAL SNSIGPVRDG
SPDALQNPCY IGSHGCDSNA ACRPGPGTQF TCECSIGFRG DGRTCYDIDE CSEQPSVCGN
HAICNNHPGT FRCECVEGYQ FSEAGTCVAA VGLRPVNHCE TGLHDCDIPQ RARCIYMGGS
SYTCSCLPGF SGDGRACQDV DECQPSRCHP DAFCYNTPGS FTCRCKSGYQ GDGFHCVPGV
VEKTRCQHER EHILGTADSS RPRPPGLFVP ECDEHGQYVP TQCHSSTGYC WCVDRDGREV
QGTRTRSGMR PPCLSTVAPP VHYGPPVPTT VIPLPPGTHL LFAQTGKIER LPLEGSTMTK
SEAKTLLHAP GKVIIGLAFD CVDKMVYWTD ISQPSIGRAS LHGGEPATIV RQDLGSPEGI
ALDHLGRNIF WTDSQLDRIE VAKLDGTQRR VLFETDLVNP RGIVTDSVRG NLYWTDWNRD
NPKIETSYMD GTNRRILVQD DLGLPNGLTF DAYSSQLCWV DAGAHRAECL KPGQSSRRKV
LEGLQYPFAV TSFGKNLYYT DWKTNSVVAV DLAVSKETDS FHPHKQTRLY GITSALSQCP
EGHNYCSVNN GGCTHLCLAT PGSRTCRCPD NTLGVDCIER K
//
