ID A0A401PJP4_SCYTO Unreviewed; 1249 AA.
AC A0A401PJP4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Nidogen-1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0002489 {ECO:0000313|EMBL:GCB73342.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB73342.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB73342.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB73342.1}.
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DR EMBL; BFAA01000626; GCB73342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PJP4; -.
DR STRING; 75743.A0A401PJP4; -.
DR OMA; PGTGNQF; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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:0007160; P:cell-matrix adhesion; IEA:InterPro.
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; 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; PF12947; EGF_3; 2.
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; 1.
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; 4.
DR PROSITE; PS50026; EGF_3; 5.
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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1249
FT /note="Nidogen-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019328595"
FT DOMAIN 101..268
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 397..437
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 441..674
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 675..716
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 717..759
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 764..807
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 808..844
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 852..922
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 993..1035
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1036..1078
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1079..1123
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 892..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1249 AA; 138344 MW; 3954F669841EE265 CRC64;
MLRTGMVWRL LLAPLLLQAA AVSGLALRDL LPHGEGAGDQ LLAAGDDVTS ESVRLAQAVR
LFDRTVRNLY VNTNGIIAIS KPPKEMEYVD TFPPKFGAVV PFLADLDTSD EVGKVYYRED
SSPHTLRRVA LMVNKAFNEL RFNPDNVFIA TWKNVTAHEE PRRGDQPQKK RNTFQVILTS
DESSSYAILL YPEGGLQFYG TRSKAANNID LELPARVGFS RGESSFVLFT LEWPSYAVTS
SSEQSVKNLY QDSNSGERGV WVFQLGSSSN HTIVPASVNL VDDSVPDTFS TATTVDRQWN
SYLDVIENGS DPENDVPEEE EKIGTLEEAV DYRVASQHNV ENLPPEEPRY EEQVPVLSRI
EAKPVQFQHP HFPQRRVELL DSELDVTGNV FSYSTERQLT CANSRHICSI HGQCSDYVAG
FCCHCNPGYY GNGKQCVAEG SPQRVNGKVN AKIFVGTSPV PVQFENIDLH SYVVVNDGRS
YTAISRIPAA LGWSLLPLSS VGSIIGWMFA LEQPGYENGF SVVGGEFDRR AEVTFTPGNE
KLTINQHFSG IDEHNHLTIT TSLEGRVPEI PQESTVHIEP YNELYHYSSS AIMSSSNIQY
TVEFPGGTSR GYSFQLKQTI SFHGCIHDDD ARLVPTTQQL SVDRTFVLYD KNEQILRYAM
SNKIGPVQDD SSSPNQNPCY TGTHGCDTNA ACRPEQGNRF ACECSAGFYG NGQTCYDLDE
CRDNLSICGN YAVCNNQPGT FRCECFAGYQ FAEDGRTCVA VQRPDNPCQT GTHNCDSPGR
ARCIYTGGSD FICACLTGFS GDGKSCVDLD ECQPNRCHPY AQCYNTPGSF SCRCSPGYQG
DGFQCAPIDS QKTECEFRRD SSRSILTPRG HRPDSYYIPE CDVHGNFVPV QCLYSQESCW
CVDTNGNEVA GTRTGRGVRP PCLETVTPTP AVGPTTRPDV IPLPPGTHLL YAQSGKIDHI
PVEGSSLKKN KAKTLLHVPD KVVIGIAYDC VDKMVYWTDI AGHTISRASI QGGEPTTIIE
IDLKSPEGIA VDHLGRNIFW TDSGLDRIEV AKMDGDQRRV LFTDDLVNPR AIVVDPVNGN
LYWTDWNRDA PKIETSYMDG TNRRILVKDD LGLPNGLTYD PYSALLCWAD AGTQRLECMN
PNRTGRRRVI DSIRYPFGIT SYGRNLYYTD WRRESIIAVD RNIGRESDEH QPSKRSRLYG
ITTAYSRCPP GQNHCAVNNG GCTHLCLATP LSRSCRCPDG SGISCVERN
//
