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Database: UniProt
Entry: A0A0V1HCE9_9BILA
LinkDB: A0A0V1HCE9_9BILA
Original site: A0A0V1HCE9_9BILA 
ID   A0A0V1HCE9_9BILA        Unreviewed;       948 AA.
AC   A0A0V1HCE9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Very low-density lipoprotein receptor {ECO:0000313|EMBL:KRZ08122.1};
GN   Name=VLDLR {ECO:0000313|EMBL:KRZ08122.1};
GN   ORFNames=T11_7935 {ECO:0000313|EMBL:KRZ08122.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08122.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ08122.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08122.1};
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   -!- 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:KRZ08122.1}.
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DR   EMBL; JYDP01000091; KRZ08122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HCE9; -.
DR   STRING; 268475.A0A0V1HCE9; -.
DR   Proteomes; UP000055024; 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; 8.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 8.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 4.
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:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:KRZ08122.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KRZ08122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..948
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006879043"
FT   TRANSMEM        839..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..362
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   DOMAIN          365..404
FT                   /note="EGF-like calcium-binding"
FT                   /evidence="ECO:0000259|SMART:SM00179"
FT   DOMAIN          368..404
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   DOMAIN          405..444
FT                   /note="EGF-like calcium-binding"
FT                   /evidence="ECO:0000259|SMART:SM00179"
FT   DOMAIN          408..444
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          541..583
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          584..626
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          627..671
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          727..778
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REGION          809..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        36..54
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        48..63
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        152..164
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        159..177
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        211..226
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        296..311
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        322..334
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        329..347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   948 AA;  105030 MW;  E664EB649D115D8F CRC64;
     MTMKSIFLYI CASIFISFHI SLATDKDCLN NGGFLCPSGR CISPSWLCDG EQDCEDNADE
     QNCSDRTCRK GEFKCANSNK CIPQSWVCDS SIDCTDRSDE DPTICTKHHC PSDHFRCHLD
     GKCIPLTWVC DSHPDCVDGS DELSNMCVKH PCNETEFSCK NERCIPKEWE CDRDDDCGDN
     SDEHDKCSYH CDPKSFQCVE SGKCIPYEYV CDGQMDCSDR SDEMNCKQLT KLPEHHSCRA
     HEFQCQDGAC INERFVCDGD VDCPDMSDEM NCLSNCSALH FRCASGKECI PSVYRCNGIA
     DCGDGSDEKN CASESVGEVK HCSAKQFDCG NGFCIDWDVV CDGKQDCPGY KVVDEEPLLN
     CSLKGTDFCK EKPCEQLCTN TPIGPQCSCR PGYTVSLTNP KQCNDINECN TAGKCSQICI
     NTVGSYTCKC YDDYVLLNNK RSCRANGPQP KLLLTNRLSI RQFGLISLTP EMLVNNLNSV
     VAIDYLYKKR LLFWSDISKE QIFSCQFGND FHAINASDCE RPIISNNVSS PDGLAVDWIH
     DLIYWTDTGM DTISVATLDG KLRHTLIRDG LDEPRAIAID PSCGMMFWTD WGVSPKIESA
     AMDGTNRFAI DRDVIWPNGL TLDMLEHRLY WVDAKLKQIC SSNYFGQDKK VILNSRNRIY
     HPFSVSVFEE TLYWTDWNSE GVHMANKFTG ENNRPLLKGM FGLMTVKIFH PVAQPNCNTF
     KPSRENKCEN SECAHLCVPS MKIAAGQTAP AKMITNTKPY VCLCSDGYGL QANARDCIAK
     DAAATTVTID TLKKANPAAS AAAAAATTTV TTTGQGDGQG KTFTKQEHST TVKTSSSKAG
     MVLALLFTLS TIVGAVSWFV WKQRPLNVHF GQFFCLSYPF CRRGQDHYDH LRLTLDNEEY
     QSGTLISGTG SGIYQPTVKS NLGDMDAGTA LAESPMTPTV QNGGIPLA
//
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