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Database: UniProt
Entry: A0A0V0X928_9BILA
LinkDB: A0A0V0X928_9BILA
Original site: A0A0V0X928_9BILA 
ID   A0A0V0X928_9BILA        Unreviewed;       591 AA.
AC   A0A0V0X928;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 1B {ECO:0000313|EMBL:KRX84318.1};
DE   Flags: Fragment;
GN   Name=Lrp1b {ECO:0000313|EMBL:KRX84318.1};
GN   ORFNames=T06_11664 {ECO:0000313|EMBL:KRX84318.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84318.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX84318.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX84318.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
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:KRX84318.1}.
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DR   EMBL; JYDK01000007; KRX84318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0X928; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd07066; CRD_FZ; 1.
DR   CDD; cd00112; LDLa; 6.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
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; PF00057; Ldl_recept_a; 8.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM00192; LDLa; 12.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 9.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 11.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Lipoprotein {ECO:0000313|EMBL:KRX84318.1};
KW   Receptor {ECO:0000313|EMBL:KRX84318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT   DOMAIN          1..128
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DISULFID        8..54
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        151..163
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        158..176
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        170..185
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        207..222
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        224..236
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        231..249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        243..258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        260..272
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        298..310
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        305..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        317..332
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        334..346
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        341..359
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        379..397
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        436..451
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        453..465
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        460..478
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        472..487
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        497..515
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        509..524
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX84318.1"
SQ   SEQUENCE   591 AA;  68026 MW;  269DA9F0A66F32C7 CRC64;
     LFDLVPFCTD FGWQKTCYPN HLGYRNKYEV LASLSFFQIL NKQQCHKHVQ IFACLLLQPP
     CKENTGIVSV CRPFCEEVVS ACSKSLEMTE IGEKNLCSDV ISNYGPNCMQ FCDKDDFICE
     QTRLCINATR RCDGNLDCGA NDISDELNCE CKSNEFRCRN GLCISQSKTC NNENDCGDWE
     DEKNCTCREN WKKCTETGQC FPASFWCDGE FHCGDKSDEL QCECPREQFI CQNGACMPKN
     VRCNGVNDCG DFSDEFDCEC QAEQFRCDKY LCKYFDNDWC NGKADCVDGT DEPANCTCKP
     GQFKCDDGFC LAKHRVCDRY IDCKDGSDEL HCDCTPEEFQ CEPGICIPVE KVCDGEANCA
     NRKDELQQCE CNSKEQFRCK NGQCMNINRY CNHRTDCLDG DDEFQNCEGK CPPGYGKKCN
     LRTTGEYKCL PESMMCDGVS DCERNEDEEN CKCREDQFQC NDGACKPWSL YCNSIHDCLD
     FSDETNCTCN EKYQETCHDG WCYDKNHRCD GKAQCADLSD EYNCTCAEYL RKSNPEKLCD
     YVQDCADRTD ELNCSTHYSI TTHKQTDKYI YINYFRNLFK FFRLHPKQLE K
//
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