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Database: UniProt
Entry: A0A443S8T6_9ACAR
LinkDB: A0A443S8T6_9ACAR
Original site: A0A443S8T6_9ACAR 
ID   A0A443S8T6_9ACAR        Unreviewed;       568 AA.
AC   A0A443S8T6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=B4U80_13292 {ECO:0000313|EMBL:RWS23927.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS23927.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS23927.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS23927.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(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:RWS23927.1}.
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DR   EMBL; NCKV01005655; RWS23927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443S8T6; -.
DR   STRING; 299467.A0A443S8T6; -.
DR   EnsemblMetazoa; LDEU008113-RA; LDEU008113-PA; LDEU008113.
DR   VEuPathDB; VectorBase:LDEU008113; -.
DR   Proteomes; UP000288716; 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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 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; 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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00135; LY; 4.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS51120; LDLRB; 3.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124};
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:UP000288716};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..568
FT                   /note="EGF-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019580703"
FT   DOMAIN          73..113
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          256..299
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          300..343
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          344..386
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        44..62
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   568 AA;  65150 MW;  F18733AF4BD08989 CRC64;
     MNKITSFLNV IFIITFTQKV NVTVLFYGDY DNAEECNVKS EFKCWNKRCV FNNQVCDGFD
     NCGDNSDEPW NCNINECKSK HNNCGHRCID DKIGFHCDCF LGYKLNNKTN KCEDVDECLG
     ITSVCGNMSC FNVHGSFECD CGENKTVHSL YPCKRQENEK PFILFVTNED IRFTNISFYA
     MDINALDQLY HNVSKAVAVD YSLRSNYILW SDVSENKLFI GKFNKSKPSK FSNTKRIFLE
     SDLKGVDGIA VDWIHDLLYW TDRDRKTIEV CSINNPNDTR SVLITELDKP RGIAVNVVQS
     FIVWLNCGQQ PKIERAAQDG SNRKIIVEKD LGNPNGITID YTEKRIYWLD TAISKISACD
     FDGSHREIIL HSPHYFSEAF SINVFESVIY GSSRKLGLIF RFIKISENEY KFKPTIINAK
     SINDLKIVHE SKQPLTHNRC KSSKCSHLCL PHNETCSVCI CPVNHILKID GLSCVKNVTE
     NHHTSERYSF FKKVKIKASR ISNANCFNEF ESNGINNHDQ IEEKHILYFV ISLEQVSGDV
     YFKIIVMYLA NQKNLTADNF NTTEITIV
//
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