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Database: UniProt
Entry: V5HL05_IXORI
LinkDB: V5HL05_IXORI
Original site: V5HL05_IXORI 
ID   V5HL05_IXORI            Unreviewed;       435 AA.
AC   V5HL05;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative prolow-density lipoprotein receptor-related protein 1 {ECO:0000313|EMBL:JAB84415.1};
DE   Flags: Fragment;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB84415.1};
RN   [1] {ECO:0000313|EMBL:JAB84415.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB84415.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; GANP01000053; JAB84415.1; -; mRNA.
DR   AlphaFoldDB; V5HL05; -.
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; cd00112; LDLa; 6.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF67; PROLOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1-LIKE PROTEIN; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00057; Ldl_recept_a; 6.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 6.
DR   SMART; SM00135; LY; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 6.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 6.
DR   PROSITE; PS51120; LDLRB; 1.
PE   2: Evidence at transcript level;
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   Lipoprotein {ECO:0000313|EMBL:JAB84415.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:JAB84415.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          250..290
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          377..422
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        2..14
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        9..27
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        53..71
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        129..141
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        136..154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        169..181
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        176..194
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        215..227
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        222..240
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        234..249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB84415.1"
FT   NON_TER         435
FT                   /evidence="ECO:0000313|EMBL:JAB84415.1"
SQ   SEQUENCE   435 AA;  48353 MW;  4A4319FCE8224322 CRC64;
     SCPAMSFRCL NGLCIPDSWR CDRDMDCEDG QNGTLSSDEL DCEYKCARDQ FQCKDGECIS
     LLSRCDGHPD CSDSSDEPPA CRVRPCGENE FKCNSTGQCI PKAWMCDGAG DCSDGSDEHL
     DLKCPVRTCK PSEFRCLNQV CIQESYYCDG DQDCEDGSDE PSTCEKRRCR EDQFTCGNGR
     CISRHALCNG WEDCRDGSDE RSDVCHEADP KVSGCPEGHF KCANKICVNE SLLCNGENDC
     GDFSDENRCN INECELSTHA CWQVCEDLPI GYNCSCHPGF KPKNEGRICE DVDECATQYP
     CTHFCRNTYG SFACSCADGY FSVDGGRTCK ANSPVKASLL LSNRYYIRQV DLHRMSSDIL
     AQNLTNSVAL DFDSVDNCIY WSEVTAVGSS IKRMCLNGSQ EHQVLHSTTV QNPDGLAVDW
     VGRNLYWCDK GKDTI
//
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