ID A0A0K0E677_STRER Unreviewed; 922 AA.
AC A0A0K0E677;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=EGF-like domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000500800.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000500800.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000500800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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; A0A0K0E677; -.
DR STRING; 6248.A0A0K0E677; -.
DR WBParaSite; SSTP_0000500800.1; SSTP_0000500800.1; SSTP_0000500800.
DR Proteomes; UP000035681; 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; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
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; 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; 6.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 2.
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:UP000035681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..922
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005327626"
FT TRANSMEM 827..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 433..468
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 578..620
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 621..665
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 894..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 37..49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 44..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 56..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 122..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 167..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 188..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 195..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 207..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 247..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 293..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 331..346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 437..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 922 AA; 103404 MW; 376A85F6C8CE4132 CRC64;
MNTRLIYLVL SILITLSFGK LIPSTHGSYT GHIPITCDDD SFYCKDGTCI QRSWLCDGEK
DCNDGSDEEN CGTLNPSIFC KNKTEFFCHK SLISKYSDTS MNLGHSSHSF RETYCIPKDY
HCDGHDDCEN GEDEEHCDGN ITCSDGTFKC PQSENDKSTC VPIAWKCDGS QDCFDGSDER
NCSMSASCLE SQFLCDNGQC IYEKWVCDGE KDCNDGTDEA KCHEECNTET HFKCKDGTRC
LPLHLRCDGD ADCVDHSDES DCNSFNPIHT RTCNAGEFQC ASNTRCISAS WRCDGDVDCA
DGSDEKGCEE KTCTVDQKKC DNICKPKDLW CNGVVDCNDG TDEINCVFPH SSITACNPTT
QYECSETPKM CINYEDLCKD NLSSNNCITS ICNKHIHSCK KDSPNCQCRD TKFNGSICYC
KKGFELQNEY CVDINECNNE GTCDQICHNT PGSYECDCYH GFQLVRFDNK SIIPHKCRAS
GSDPLLLLTN RASIRQYDMT KHVVSPLISS LKSAVAMDYW HKNGIVTWSD LVNEHIMSCQ
MDHKEPVYNI SKCTDGNGTI LVKNVTNADG LAVDWVHGLL FWTDSIKKHI SVVDIKTGKN
KILFNTSLDE PRAIAVDPAS GLLFWTDWGK HAKIERAGMD GNHRTVIASG EHIKWPNGLT
LDILDKRIYF ADAKVKSISS MDYWGNNLRT VIHSHEKLKH PFSLAVFEEK LYWSDWDRDG
IVSANKFSGS DVTEVLRHVS TPMTVRIFHE AVQPDHPDKC QANRCSGICL PKAHYRTDVE
EQKKMNDELP YSCVCDDGSI LINEVCVLNH AVSDFIKDST RGKTSTIVVF LLLTGAVGIM
GYTFYSRRKR PVNQFVRFSN PVYRTTIEDG SHDMDEINDR SIVNITRTLP NTTNSLVDNT
TNQSNIDPSL SFSNPTFGGN RE
//
