ID A0A0M9A5Y8_9HYME Unreviewed; 1673 AA.
AC A0A0M9A5Y8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Vitellogenin receptor {ECO:0000313|EMBL:KOX76539.1};
GN ORFNames=WN51_11745 {ECO:0000313|EMBL:KOX76539.1};
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:KOX76539.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX76539.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX76539.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX76539.1};
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:PRU00076}.
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DR EMBL; KQ435746; KOX76539.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M9A5Y8; -.
DR OrthoDB; 2877710at2759; -.
DR Proteomes; UP000053105; 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; 10.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 10.
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; 8.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00192; LDLa; 10.
DR SMART; SM00135; LY; 11.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
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; 7.
DR PROSITE; PS50068; LDLRA_2; 10.
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:KOX76539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1564..1584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..200
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 244..288
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 332..375
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 376..418
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1410..1452
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1654..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 45..63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 57..72
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 165..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 872..890
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 884..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 904..916
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 911..929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 923..938
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 943..955
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 950..968
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 983..995
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 990..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1002..1017
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1048..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1066..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1073..1091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1085..1100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1121..1139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1673 AA; 188894 MW; 843DEB56F30D6567 CRC64;
MLDVATAMEQ TTVTQLTGIC YFPVYTFSIV MSKDSPTLQC DRFKCKDGHC IRNEWICDGV
PDCLDKSDEE NCENSMIPVD KCNNEYDRYL CKNKRCIFLN ATCNEKDDCG DNSEENVDAC
KKADTACKEA QCQHNCRKTP VGAQCSCRSG YKLMNDQTCE DVNECDNYGT CDQKCINNAG
SYTCTCQSGY NLDDDKKTCK VEGGEAEMVF SIKSEIHGVY LSSEIYYPIT RNLQHAVAVS
LDANYIYWSD IENGNEAIIR SSVDGAQREI IVTTGLNNPD DMAVDWVTGN VYFTDSGYMH
IGVCSNDGSY CTVIIEEPND KPRSLALLPS SGIMYWSKWG VNSCILKAGM DGKNNTVLIN
ENLKLPNSLA IDYANNRLYW IDIKTKIIES ARLDGTDQRV ILQGVAKKPF SLAVFENKLY
WSDWISNTIQ SCDKFTGKNW KILVDTNSTI YGIHIYHSVL KPKMPNPCNS NPCSQLCLLN
SENGYTCACT LDKELNHDNH TCRAVKKKVH LVIATGNTFI DYYHELLGKP KMTTNVILNH
ITEIAYNPLT GGLLASDQLR DNIFHFDTHT DDLKSLISIE NEILGGMDFD YLGNNLYLSD
MKHKTIEVHN LDNNEKTIFY FQDEPYDIAL VPEEGIMIVV FNADKSYRID LMNMNGLGPR
TTIEGNKTPL IGPKVSLCYD RDLKQLFWSD QGTGRIGITT IPGLETYIFR TGLSEPVSLA
VLGNYVFWTQ YKSDQLYWTK KSNIQQYQKH ITLKITPNNL DRIQLVGIHE TYVKEHQCRI
NNGNCSHVCL LSNSHSYLCA CPPDMMLNVD NRTCSPQTAC NAGEIKCSEH DVCIKFDQKC
NGVQDCPNGE DESSICDEYH WSKCKHQDQF QCKNGECISK TKRCNSYYDC ADWSDEEGCD
KKECDSNEFQ CHEGACISKY LVCNGQSDCT DFSDELNCDK HECDADSFTC ETGTCIPKTW
ECDGEVDCAD RSDEHETCQR NACPSEMFTC LSGRCIDLIL KCNGISDCED NSDEQYCNYV
GNNNYVNCSA DQYKCFNTEL CLPNEVRCNG ISDCPKNDDE RNCARCQKEE YVCNNQKCID
KNWVCDRIND CGDGSDEKDC DGGNSRMNSV SSISKCKEFK CSNGVCLPFA KVCDGKVDCS
DQSDEYGECK IACTKVNPCT NVCHKTPTGP VCGCRNGYQL NNNLKFCEDI NECENNVCSQ
LCHNTNGSYI CSCYEGYVIR SDKTSCKVAG PQMEIITVSG DDIRKLSPNL NSIEVIYEEI
NFEINGIDVN TKENTIYWSN DVLGMISKIN MKTKERKTVT GLGNPEALAV DWITDNVYFN
DNDRSSSIQV CNLEQQKCAK VVSITQKYRA ISIAVEPKKG WLFWSQTIWS DYDRPMTEIY
RSSTIGTNAT AIVHHYLGIV FALTIDYTRS KLYWSNTFHK TIESSNLDGS NRVVVLNTLI
YQALSISIYE DSLYWLISTT GTIRKCKLYG DKSCTTIIIG ISNIDKHFII SHTIKQPVGK
NFCETHDCSY MCVSGNNGFA CICHDGYPTD SKNICTENTN TKIKFNSNIA SYRNESIRHQ
QGTLAGIIIT VLACFIVASA YFYYQKIKPN FSKKNNLSIH FQNPSFDQRN EINFISGLPP
GEHEYVNPVT NIQQNKNENI TEKNEKQIMK MFNFDQSDDE SKESMNKQDI RLI
//
