ID A0A6I8P0H5_ORNAN Unreviewed; 1221 AA.
AC A0A6I8P0H5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Nidogen 1 {ECO:0000313|Ensembl:ENSOANP00000046049.1};
GN Name=NID1 {ECO:0000313|Ensembl:ENSOANP00000046049.1};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000046049.1, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000046049.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000046049.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOANP00000046049.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000046049.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {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 AlphaFoldDB; A0A6I8P0H5; -.
DR Ensembl; ENSOANT00000073995.1; ENSOANP00000046049.1; ENSOANG00000001218.3.
DR GeneTree; ENSGT00940000156318; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000001218; Expressed in heart and 7 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 1.
DR FunFam; 2.10.25.10:FF:000038; Fibrillin 2; 1.
DR FunFam; 2.10.25.10:FF:000014; Latent-transforming growth factor beta-binding protein 3; 1.
DR FunFam; 2.10.25.10:FF:000297; Nidogen 1; 1.
DR FunFam; 2.120.10.30:FF:000030; Nidogen 1; 1.
DR FunFam; 2.40.155.10:FF:000001; Nidogen 1; 1.
DR FunFam; 4.10.800.10:FF:000001; Testican-3 isoform 2; 1.
DR Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; IPR050778; Cueball_EGF_LRP_Nidogen.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; IPR024731; NELL2-like_EGF.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR049883; NOTCH1_EGF-like.
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; 1.
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; 5.
DR SMART; SM00179; EGF_CA; 3.
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; 2.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
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 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..283
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 450..688
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 683..725
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 732..775
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 776..814
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 820..893
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 964..1006
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1007..1049
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1050..1094
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 316..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 863..870
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1221 AA; 132941 MW; AA392CEF4DA982C5 CRC64;
MGRGQGSPPR RLPGVLLSWP LWGLLWGLLL GLLLGLPGPG LCLSRRDLFP YGPDHGDLQL
QPGHRGLAPP LPLRRPLRFY QQEGLRNVYV STNGYIATSQ PPEKEVYPGR FPPTFGAIAP
FLADLDITDG RGKVFYREDS SPAILQLAVD CVLRGFPDLQ FHPLSAVVVT WESVAPYLGP
DGVAAQEDQR NTFQAVLVSS DSSSYAVFLY PEDGLQFYST RSKDTGDPVS ATVGFSQGSQ
VGLFWTSDGA YNIFANDRES LENLAKSSNS GRQGIWVFEI GSPATASGVV AADVGSGPDS
ADYEDEDEFD YDATIGFRRF PGGENPTPSP DDIATAGGHG EWSPSPASPE RPSAEGPTTS
PAPELSTAWT QAYRFQARSF PQQPPQVIDV DEVEETGIVF SYNTDSRQTC SNNRHQCSVH
ADCRDYATGF CCSCVAGYTG NGRQCVAEGS PQRVNGKVQG TIYVGSRQTP FVLDNTDLHS
YVVMNHGRSY TAISTVSEAL GPSLLPLAPL GGIIGWMFAV EQQGFKNGFS ITGGEFARQA
EVTFLGQGEK LLIKQQLKGI DEHGHLTIST ELEGRVPEIP SGSTVHIEPY TELYHFSDSV
ITSSSTREYT VTEPERDGGG AQTYTSTYQW RQTITFQQCS HEDSQRALPA TQQLTVDSVF
VLYNQDERIL RYALSNSIGP IHDINECVEQ SEACSRNAVC HNYPGTFRCE CLEGYRFADD
SRTCVATDDE RPTNYCENGL HDCDIPQRAQ CVYTGGSTYI CSCLPGFSGD GQACEDVDEC
QQRPCHPDAS CHNTPGSFTC RCQAGYAGDG FRCVPGETEK TRCQQEREHL LGAAGALDPR
GPRPVSIFVP QCDEHGNYVA TQCHGSTGSC WCVDRHGSEI AGTRTGPGMR PPCLSTVAPP
LHPGPSVPPA VIPPPPGTHL LFAQTGKIER LPLEGNGMKK AEAKALLHIP DKVIIGLAFD
CVDQVVYWTD ISGPSIGRAS LHGGEPDAII GQGLGSPEGL AVDHLGRNLF WTDSQLDRIE
VARLDGGLRR VLFESDLVNP RGIVADPVRG NLYWTDWNRE SPKIETSYLD GTHRRVLVKD
DLGLPNGLTF DPHSSLLCWV DAGTHRAECL NPSQPDRRRI LGGLQYPFAV TSFGKDLYYT
DWKMNAVVVV DRHASKETDT FHPHKQTRLY GITTALAQCP QGHNYCSVNN GGCTHLCLAT
PGSRSCRCPD NTEAVDCVER K
//
