ID A0A401NIZ0_SCYTO Unreviewed; 865 AA.
AC A0A401NIZ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=scyTo_0014232 {ECO:0000313|EMBL:GCB60829.1};
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:GCB60829.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB60829.1, 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 -!- 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:GCB60829.1}.
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DR EMBL; BFAA01007567; GCB60829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401NIZ0; -.
DR STRING; 75743.A0A401NIZ0; -.
DR OMA; LSTCWCL; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR24270:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 6.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..865
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019540161"
FT TRANSMEM 793..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..395
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 441..487
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 488..530
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 531..574
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 575..619
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 29..41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 36..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 199..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 206..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 218..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 238..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 245..263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 257..272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 286..304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 360..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 865 AA; 96250 MW; F8BC7626AFE03333 CRC64;
MAKVFALLLL LTVHSLEDVV GAATATGLCD QNHFRCGDGK CIRAHWLCDG QSECADGSDE
SLETCKNKTC SALEFSCGGR VNKCIPRSWR CDSQKDCENG SDEENCPAHK CEDNEFQCHD
ENCISVQFVC DEESDCTDGS DEVGCPERTC GPHMFQCAES KICIPKLWAC DEDPDCPDES
DEWPQNCGQS PKSEPPNPCS SLEFHCGSGE CIHMKWRCDA TADCRDQSDE QGCAVATCRP
DEFQCNDGTC VHGSLQCNKE FDCHDKSDEA GCVNVTKCDS PHKFKCMSGE CIMLDKVCDK
QRDCRDWSDE PLKECGENEC LNENAGCSHI CQDLKIGYKC LCRPGFRLVD NANCEDIDEC
ENPDTCSQNC INLEGGFKCE CNEGYHMDPV TSQCKAIGTV AYLFFTNRHE VRKLTLDRSE
YTQLIPRLKN VVALDMEVAA NKIYWADQFQ KKIFSAHMDK AENSSHHSTV IETEIKAPDG
LAVDWIHQNI YWTDSETSTI SVANTAGTKR KVLVKDQLSK PRAIVVDPIH GFLYWSDWGY
PAKIEKGGLN GVDRMPLVTT GIEWPNGITL DLVNQRLYWV DSKLHTLSSI GVAGDNRKTL
IISPDKLAHP FSVALFEDKI FWTDIDHEAI FSANRLTGDD ILTVIENLDV PQDIVLYHHL
RQPKGINWCE LNGQVNGGCE HLCLPAPQIN VHSPKYTCVC PDGMQLGPDM RSCIPATIMP
TNKLSTVKTL TNPNRVETFT TRKMITSQPS NVPPDHAEPT VVPTLHEMLT VSHQALGEVA
AEAAAEGHKG INALWIVLPL AILSLLGTAA YFIWKNWRLK NTNSINFDNP VYQKTTEDDE
VHITQSQVGY TYPTRAVVSL EDYGA
//
