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Database: UniProt
Entry: A0A0L7QUY6_9HYME
LinkDB: A0A0L7QUY6_9HYME
Original site: A0A0L7QUY6_9HYME 
ID   A0A0L7QUY6_9HYME        Unreviewed;      1711 AA.
AC   A0A0L7QUY6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Vitellogenin receptor {ECO:0000313|EMBL:KOC62359.1};
GN   ORFNames=WH47_03772 {ECO:0000313|EMBL:KOC62359.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC62359.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC62359.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC62359.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
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:PRU00076}.
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DR   EMBL; KQ414731; KOC62359.1; -; Genomic_DNA.
DR   STRING; 597456.A0A0L7QUY6; -.
DR   EnsemblMetazoa; XM_017937688.1; XP_017793177.1; LOC108574999.
DR   Proteomes; UP000053825; 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; 12.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 12.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00057; Ldl_recept_a; 12.
DR   Pfam; PF00058; Ldl_recept_b; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00192; LDLa; 12.
DR   SMART; SM00135; LY; 11.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   SUPFAM; SSF57424; LDL receptor-like module; 12.
DR   SUPFAM; SSF63825; YWTD domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 12.
DR   PROSITE; PS51120; LDLRB; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KOC62359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1711
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005574904"
FT   TRANSMEM        1633..1656
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          235..274
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          318..362
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          406..449
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          450..492
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1480..1522
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        33..51
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        45..60
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        79..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        118..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        130..145
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        164..182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        239..249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        942..960
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        954..969
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        974..986
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        981..999
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        993..1008
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1013..1025
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1020..1038
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1053..1065
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1060..1078
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1072..1087
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1118..1133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1136..1148
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1143..1161
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1155..1170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1191..1209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1711 AA;  192858 MW;  9A17B16CB135A511 CRC64;
     MYRKLFVVLV LSTIYTHIDT SIIRCDAPEW FSCDNKKCIS SVFRCDGEND CGDDSDEIHC
     QGIQIAPETI RCATDEFQCF DRSCIPIEKF CDARPDCPDE SDEYDNCVKD LKCDTFRCND
     GHCIRNEWVC DGVADCPDKS DEGKCDNQTI PIDQCTNNYD RYLCKNQRCI SLDLTCNGKD
     DCGDHSDENV DQCKKAVETC KQTAKCEHHC RKTPEGAQCS CRSGYKLMDN RTCADVNECE
     EYGRCDQRCV NTLGSYICLC QSGYLLNDDK KTCKAEGGEA LMVFSIKSEI HGYYLDSQVY
     YPVTRNLQHA VAVSLDANYV YWSDIENGDE AIFRSLEDGS EREVIVTTGL SSPDDIAVDW
     VTGNIYFTDS GYMHVGVCNN DGSYCTIIIK ERNDKPRGLA LLPSSGLMYW TEWGMNSCIL
     MAGMDGKNST VLIEKDLEWP NSLSIDYANN RLYWIDSKLK VIESIRLDGT DRRIVLKGVA
     KKPFSLAVFE NKLYWSDWIS NTIQSCDKFT GKNWEILVNA NSTIYGIHIY HSILKPKLPN
     PCNSNPCDQL CLLNSENSYT CACTVDKELN SDQRTCRAMK KKAHLVIAAG NTFIDYYHEL
     LGKPKITSSA TLKHVTAVTY DPFTGGLLAS DQLTDMIFHF DTQTGEVKTM MPIEDKLLGG
     MDFDYIGNNL YLLDVKHKTI EVHSLNTSEK TTFYFQDEPH GIALIPEESM MMVVFNVDGK
     YQIDMMKMNG LGQRITIKSQ LYGPKVSLCY DRDLKRLFWS DQGTGRIGST TVPGFETNLF
     RTGLSEPVSL AVLGDHVFWT QYKSNQLYWT SKSSTQQYQK RITLRTPTEL DRMQLIGLHG
     TYVNEHQCRK NNGNCSHVCL LSNPHSYICA CPPDMMLNGD NRTCSPQTAC KPGEVKCGEH
     DICIKSYQRC DGVRDCPNRE DESSVCEEMH WSKCKHEDEF QCKSGECINN TKRCNSYYDC
     ADQSDEEGCD KKECNSNEFQ CHEGACISKY LVCNGLNDCS DATDEINCSK HTCDTDSFAC
     ESGACILKTW KCDGEVDCPD GSDESDECQR VGCPSEMYTC SNGRCIDSML KCNGIDECED
     NSDEKYCSDF GNKNPVNCTV DEYKCFHTEM CLPKRVRCNG VQDCPKYDDE RNCVRCLPEE
     YVCDNQKCID KSWVCDTVND CGDGSDERDC DGGNSRTNDV SVISNCKEFK CSNGVCLPFD
     KVCDGKADCL DRSDEFGECA IACTKNNPCS NMCHRTPVGP VCSCRSGYKL SSDLKSCEDI
     DECKENSCSQ ICHNTKGSFT CSCNEGYIIR GDRTSCKVAG PQMEIIAVAR NDIRKLSPNL
     NSIEVIYEEM NSEISGIDFD ARGETIYWSN DVLGMVSKIH IKSKERKTVT GLGRPEALAV
     DWITDNVYFN DNDHFSTIKV CNLEQRKCAK VVSIGSKNRA TAIAVDPRQG WLFWSQTTWT
     FYDKPTTEIY RCHTTGTNAT AILYRDIGAV FAMTVDYARS KLYWSDTFLK SIESSNLDGS
     NRKLVLNTDN YQALSISVYE DSLYWLMAPT GTVKKCKLYG DKSCTTIPIG NSNVDKYFTI
     LHTIRQPIVK NSCEKYTCSY MCVHGKDGPA CICHNGYTKD SNTCMQDTNN KIQFDSSIAS
     RRNKDVRQQN GTLFGIITMI LIGLACIVLG LTYFYFRNIK PNCLKKNSLS IHFHNPLSEH
     NEDTFLRNCI SGLPTGEHEY VNPLTDIQKV E
//
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