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Database: UniProt
Entry: W6UNK1_ECHGR
LinkDB: W6UNK1_ECHGR
Original site: W6UNK1_ECHGR 
ID   W6UNK1_ECHGR            Unreviewed;       994 AA.
AC   W6UNK1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein {ECO:0000313|EMBL:EUB62793.1};
GN   ORFNames=EGR_02234 {ECO:0000313|EMBL:EUB62793.1};
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB62793.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB62793.1, ECO:0000313|Proteomes:UP000019149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24013640; DOI=10.1038/ng.2757;
RA   Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA   Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA   Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA   Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT   "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL   Nat. Genet. 45:1168-1175(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:EUB62793.1}.
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DR   EMBL; APAU02000010; EUB62793.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6UNK1; -.
DR   STRING; 6210.W6UNK1; -.
DR   EnsemblMetazoa; XM_024491483.1; XP_024353989.1; GeneID_36337949.
DR   OMA; DETTCDY; -.
DR   OrthoDB; 2996945at2759; -.
DR   Proteomes; UP000019149; Unassembled WGS sequence.
DR   CDD; cd00112; LDLa; 7.
DR   Gene3D; 4.10.1220.10; EGF-type module; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
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; PF13927; Ig_3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 6.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00192; LDLa; 7.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 6.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 7.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT   DOMAIN          893..985
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        177..189
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        184..202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        311..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        318..336
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        487..499
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        494..512
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        621..633
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        628..646
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        764..776
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        771..789
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        829..844
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        875..890
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   994 AA;  110880 MW;  E7114C11096FDC62 CRC64;
     MSKGPKYRFN KTASTAKSEQ VFPSSNLGHP KPPLIIDPRM VDMPAWQMFE FVCSSTDGSR
     VEAYFSPDDG RVGEDPRFRV KPIRHPIFVD PPHIYKPAWV AFEFVCRSST GSPIAAIFVG
     DGSRVELDPR FTVTTYNTST IIVKAPRGLR DIDDLTIQCV LPTGQKKNVT ITIASSCGEG
     YTQCDDGNCI PQTKLCDGIA QCPDHSDEDK AFCKTLLRPP VIVTPPVVEA PAWKPFQFTC
     VSTDGSQMNA VFKADGSSVY LDPRFRITRY NISALRITAP EGLRDKEDVE IECVTPTGQR
     SDVSITIFDE CERNYTKCKD GACIPETQLC DGTAQCRDRS DENPLFCKGF TCLLITKPLL
     TITIVRISAT RYDPPLDIVR ICEVFVCISG VSQRLVTVQL CYIRHPPWVP FSFVCVFPVG
     QKPDIIFADD KRSVQRDPRF TVRRVNSSSV EVTATRGLRG DQETILLECV TDGGLRGNVT
     ILIDDMCKPG SMQCRNGRCR PIAEFCDGKS DCTDESDELK EFCDVKVPNL VLTPSRVVAQ
     PWRQFRTVCV SPSGSQPTFV FSKNQSPVER DQRYLIRHIN ATSVELAAPL GLRGQEDVDE
     IKCTNAVGES VDFEVVIVSP CRAGQMTCQD GTCFPASWFC DGRYDCYDKS DERRDFCPEP
     TRTPSPRPTG VRFSPSKQRV RPGQEIRLEC SALSSDVLQH PIVEFANGTS VTVDPQFRVE
     YPQPGRSVVT IPRGAEVSQR HMEFQCYLPW SDKSRAEVFV DQVCAAGQRR CDDGHCIYLG
     QFCDGRRDCA DGSDELPHNC DACDPISRPC GVVNGEEPKV PYFQEHWRCD GENDCGNGFD
     ELNCENYTRV PGQRCGSPRY DCSSDGSQVP LAYQCDGQPD CLNGEDEMNC MRPTIYSEGW
     VSRYEVRRGQ DLVIECEVLG VPPPAIIWRF NWGCLPQSVR TRVEPVSSRF GCTGSRSRLT
     IRNVQEGDDG IYNCEGITGV DRALSQDIFV ILVD
//
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