ID B3S2H0_TRIAD Unreviewed; 718 AA.
AC B3S2H0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=TRIADDRAFT_27379 {ECO:0000313|EMBL:EDV23416.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23416.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV23416.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23416.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985247; EDV23416.1; -; Genomic_DNA.
DR RefSeq; XP_002114326.1; XM_002114290.1.
DR AlphaFoldDB; B3S2H0; -.
DR STRING; 10228.B3S2H0; -.
DR EnsemblMetazoa; TriadT27379; TriadP27379; TriadG27379.
DR GeneID; 6755539; -.
DR KEGG; tad:TRIADDRAFT_27379; -.
DR CTD; 6755539; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_008163_4_0_1; -.
DR InParanoid; B3S2H0; -.
DR OMA; GIDECAC; -.
DR OrthoDB; 3107655at2759; -.
DR PhylomeDB; B3S2H0; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
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; 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; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF5; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 4; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 3.
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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 319..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 360..399
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 493..534
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 535..578
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 579..621
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 4..22
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 16..31
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 44..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 77..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 84..102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 96..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 117..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 124..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 136..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 156..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 163..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 175..190
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 364..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV23416.1"
SQ SEQUENCE 718 AA; 79542 MW; 47725E109D99C61B CRC64;
QFACGNGRCI PIDWRCDGTD DCKDNSDETN CAQVTCHPNN EFTCNDGKCI TTSWVCDGQN
DCIDGSDEGS HCLTKTCTPD EFSCGNGVCI KRDYVCDQVD DCGNSADERN CTKVATCSPQ
QFTCNNSHCI NSAWRCDNDN DCGDNSDEWN CPNKTCGPEL FQCSSGDCIK KSWLCDGERD
CTDGSDEKNC STSRPKHTCR AGEFQCKNWE CIKSEWRCDG STDCTDGSDE LGCNKTTCKS
GQFRCSAHIC IDAHNVCDGI SDCANSRDEQ NCTTPTPPNL TCNSSQFTCH TNKSCISMKL
VCNGKFDCED KSDEPATCNI NECSEYNGHC SQNCVNTKVG YYCACNPGYT LDTDGRTCLD
INECNISNPC SQMCENTKGS YKCTCADGYR LDADFKSCKA LGPEPVLFFA NRRDIHRFTI
KGSRYNDVMK GLKGAIGIDV HVRKRLLFWT DIVSEKIGRV TLHSNGTVAG KNKYIISDGV
LSPECVAVDW IHDTIYWTDT GLDAIKMSDL DGRYVKTIIS NIADPRGLAV DPVDGYIYFT
DWGSSAKIER AKLDGTQRQI LVSTNVEWPN GLTIDYPQRK MYWVDGKHHH IESANLDGSG
RRVILSKGIP HPFSITVFEN SVYWTDWESK TVETANKLTG ANRSVLLSDL YAPMGITTFQ
LQRQPRHYDA CHLNKGGCSQ ICVKTGDYKR TCLCKDGWQL DSDGTGCVLL PSKINIDC
//
