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Database: UniProt
Entry: A0A0M8ZSK8_9HYME
LinkDB: A0A0M8ZSK8_9HYME
Original site: A0A0M8ZSK8_9HYME 
ID   A0A0M8ZSK8_9HYME        Unreviewed;      1581 AA.
AC   A0A0M8ZSK8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 6 {ECO:0000313|EMBL:KOX68763.1};
GN   ORFNames=WN51_07256 {ECO:0000313|EMBL:KOX68763.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX68763.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX68763.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX68763.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX68763.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-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}.
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DR   EMBL; KQ435916; KOX68763.1; -; Genomic_DNA.
DR   STRING; 166423.A0A0M8ZSK8; -.
DR   OrthoDB; 3107655at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR46513:SF36; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF14670; FXa_inhibition; 3.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00058; Ldl_recept_b; 10.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF63825; YWTD domain; 4.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS51120; LDLRB; 12.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:KOX68763.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KOX68763.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1365..1387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          66..111
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          112..154
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          155..200
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          201..243
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          379..421
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          422..464
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          465..509
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          510..552
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          622..637
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01186"
FT   REPEAT          684..726
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          727..769
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          770..812
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1081..1123
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          1444..1581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1550..1568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1280..1295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1298..1310
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1581 AA;  177781 MW;  FCB9F33521CDAD5F CRC64;
     MAVISLIIIL TACFFKLVLF SNGSPTLLFI TQKDIRMANA SRTNKVATII KDLSEGAALD
     FYFEHELVCW SDSGLEIIQC IQTNGTHTGE RTIIVNSSLI SPDGLACDWY TGKLYWTDGE
     KNRIEVTSID GRHRKVLFWT DIYQPRAIAL VPMKSILFWT DWGDIPKIER AAMNGDPSTR
     EVIISDDIFW PNGLTVDYEN ELVYWVDGRL KFIAVMDYYG RNKRKVIEQG LDYPFAVTFF
     DHKLYWTDWK TWCVHSYDVR QNQAHPRELL HGEYIPGDIE VWDVRRQPYG SHPCEKNNGN
     CSHLCLLSMT EPGYSCACPT GVKLVDNLTC AERPEELLLI VQRNEICRIS LDSPDYTNFV
     LPLTGIKHAI AIDFDPVQEM LYWTDEEART IRRASLDGSN QENIITTEVE NPDGIAIDWL
     ARNLYWTDTG TDRIEVARLN GTSRKVLINE DLIEPRAIAL APELGWMFWT DWNEKRPKIE
     RSNLDGTERI LLVNKDIVWP NGIALDLARW KIYWCDAKTD KIEVCNMDGT DRREVITDNL
     PHLFGLSLLG DYLYWTDWQR RSVDRAHKLT GGDREVIVDQ VPNVMGLKAV HLGKVNGTNP
     CVKSNGGCSH LCLNRPGNKY ICACQIGYEL TKDKKTCVVP DAFMLFARKE NIGRISIENA
     NNDNIIPLTG VKDASALDFN IADNRIYWTD VKLKTITRAF MNGSDIERVV DLGLEAPEGL
     AIDWIAHNLY WSDTGTRRIE MVRLEGCSRK VLIWTNIVEP RCLALDPSRG HMYWTEGGNY
     GSIERSHLDG THREIILSNI GRANGLTIDH LARKLYWADL YTPAIDSFDL RTKKRNAIIT
     DNIVYPFSIT QYQDYIYWTD WNTGDIEKAN KTTGKNRVNI HNKLESVTDL LVFHASRQAG
     WNPCALKNGN CTHLCIALPG ENESTSNFFK CECPTHYNLA EDNKTCIAPE NFMMYSLRNA
     MFRFLPDTND CPDVVLRIQG LKHVRSIEFD PITQHIYWID GRTLSIRRTL ENKTHSSIMI
     SGNSGHPVDL ALDSLGRLLF WSCAINDAIN VTKLDNGSAL GIVVKGDGEK PRNIAIHSER
     RLLFWTDVGK KMRVMRSKMD GKERVVIATD LEQPTSIAVD AMSNIVYWAH GNKIEYADFD
     GNNGGILVST IGQGSTVYLS VFFDFIYWFD KETSNLERIN KSGNERKVIM NKVLTDLIAV
     DTPQDDIMKT HICSPFRDYG GCSHFCIGTT SSKCSCPKSL VLSEDEKTCR AAPACGTDHF
     TCAAPSSAVT KDCIPATWKC DGQTDCPDGS DELGCPACSR DQFKCQSGHC IDMSWVCDGT
     AQCHDAVCDG WEDCADGSDE LPSACTPANN PRQENNSLES GRINYVIIIP IVLFAAIIAT
     FSGFCYCKRR FMNNEELPDI LHDSAGDPLS PKPVRLAKPM FAQKNCRKDL KIGMETVRMS
     MLNGSSVGSS YDRSHITGAS SSTRGSSTGG YPQETLNPPP SPATTANSTR CSSSNASRYK
     PYRHYRSINQ PPPPTPCSTD VCDESDSNYP ARYRYESEPY PPPPTPRSVY QSDAGISCPP
     SPSSRSSTYF SPLPPPPSPV P
//
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