VGR_SOLIN
ID VGR_SOLIN Reviewed; 1782 AA.
AC Q6X0I2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Vitellogenin receptor {ECO:0000312|EMBL:AAP92450.1};
DE Short=SiVgR {ECO:0000303|PubMed:15056367};
DE Flags: Precursor;
GN Name=VgR {ECO:0000303|PubMed:15056367};
OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Solenopsis.
OX NCBI_TaxID=13686;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP92450.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15056367; DOI=10.1111/j.0962-1075.2004.00477.x;
RA Chen M.-E., Lewis D.K., Keeley L.L., Pietrantonio P.V.;
RT "cDNA cloning and transcriptional regulation of the vitellogenin receptor
RT from the imported fire ant, Solenopsis invicta Buren (Hymenoptera:
RT Formicidae).";
RL Insect Mol. Biol. 13:195-204(2004).
CC -!- FUNCTION: Involved in uptake of vitellogenin by endocytosis. Expression
CC is regulated by the juvenile hormone analog, methoprene (in vitro).
CC {ECO:0000269|PubMed:15056367}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries of reproductive females.
CC {ECO:0000269|PubMed:15056367}.
CC -!- DEVELOPMENTAL STAGE: The highest expression levels are seen during the
CC previtellogenic period in virgin alate females, then decrease in
CC reproductive females. {ECO:0000269|PubMed:15056367}.
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DR EMBL; AY262832; AAP92450.1; -; mRNA.
DR RefSeq; NP_001291525.1; NM_001304596.1.
DR AlphaFoldDB; Q6X0I2; -.
DR SMR; Q6X0I2; -.
DR PRIDE; Q6X0I2; -.
DR EnsemblMetazoa; NM_001304596.1; NP_001291525.1; LOC105200757.
DR GeneID; 105200757; -.
DR KEGG; soc:105200757; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR CDD; cd00112; LDLa; 12.
DR Gene3D; 2.120.10.30; -; 3.
DR Gene3D; 4.10.400.10; -; 12.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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 Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 11.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00192; LDLa; 12.
DR SMART; SM00135; LY; 10.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 12.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 11.
DR PROSITE; PS50068; LDLRA_2; 12.
DR PROSITE; PS51120; LDLRB; 8.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein;
KW Membrane; Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1782
FT /note="Vitellogenin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378058"
FT TOPO_DOM 19..1663
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1664..1684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1685..1782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..72
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 81..118
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 122..157
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 166..205
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 208..243
FT /note="EGF-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 244..283
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT REPEAT 327..374
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 375..416
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 417..460
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT REPEAT 461..501
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255"
FT REPEAT 502..544
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255"
FT DOMAIN 552..588
FT /note="EGF-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 889..927
FT /note="EGF-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 931..969
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 973..1009
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1012..1049
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1052..1090
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1094..1131
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1140..1177
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1178..1214
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1225..1260
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1262..1298
FT /note="EGF-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 1385..1425
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255"
FT REPEAT 1471..1518
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255"
FT REPEAT 1519..1561
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 43..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 55..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 82..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 89..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 101..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 123..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 129..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 141..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 167..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 176..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 248..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 254..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 269..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 932..945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 939..958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 952..968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 974..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 981..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 993..1008
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1013..1026
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1020..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1033..1048
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1053..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1060..1078
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1072..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1095..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1103..1121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1115..1130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1141..1154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1148..1167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1161..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1179..1191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1186..1204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1198..1213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1226..1236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1231..1249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1243..1259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1782 AA; 201296 MW; 1944F8B9643031CF CRC64;
MRFIVLLFIC SFIYPCYVSS IGFRRISKVS LKKTKCEDGY FQCNSGECIP VDKKCDYIDH
CIDGSDEDFE CDHLDEKSFI TCAKDQFKCK NQECIPAAKY CDMVNDCLDE SDEHDGCVKH
LNCTNKFLCT DGHCINKEWV CDGRNDCPDG NDEWNCKANK TSSASSCKTE NYQYMCANHR
CISLKVVCDK KDDCGDGSDE GPGCTQFNCS SAGCQSNCHQ TPKGSVCTCK PGYKLQKDNR
TCNDIDECQA YGICDQDCMN VPGSYACTCQ REYYLENDKR TCKARAGEAT LVFSTRTSIL
GMHVDSEKFF SLATNLNHAV GVAMYGDYVY WSNLEENGYN TIVKKRTYHP QAPNEVIVTT
GLALITGIDV DWITKNIYFA DEDNHCIGVC TNDGTYCTVL IKDTDKPTGV ALLPTQGKMY
WSDWGTFPHI AVAGMDGKNV RIFVNVKLEW PKSVTIDYPN ERLYWVDAKS KMIESVRLDG
TDRRIVLHDI IQEPFSMTVF QNKLYWSDWE SNGIQTCNKF TGKDWKILIR NHNKPYSVHM
DHSAIKPNID NPCYSNPCSQ LCMLNQNKGY TCGCTLDKKL NADKHTCQDV KKNQHLLIIQ
GRKFINYYHE FLGKPKVMTL SLQHMSQQSY NNLVNIISDP LSGQIIICHL QLSTPFLTST
TDILRYDPVH HSSEKIVTIN KIFFELAFDY IGNNLYTTNT VNQSIEVINL NTKAMTAFYF
KDEVPKYIAL APEESKMFVA FQKSMHSISG LTLYEMQMNG LGKRKLIREG LIGPQLPMYY
DRDSKTLFVS DLLPGYIYSH SAQDTRILRS GLKSPHSLTV AGDNLFWIES QNKLYSTNFR
TASVKQKTVE FDLSKLNDNM TSLPGHLTPY SRDAQYVVTL RKDDIPKHDC QKNNGNCSHV
CLPSLITSFI CACPPGMELS NDNRTCISHH ECSKNEYKCS EHNICIQRNQ LCDGIENCPN
GEDETSECRI KGRCKENQFM CKNGDCIRLK DRCNSRYDCT DQSDEQNCEK PKCKSDEFQC
KFTETCIPKT KMCDSNPDCD DLSDEEDCRK VECTSNEFKC NNGKCIPNTF VCDNDNDCED
GEDEAAEKCY SKIACKMPKM FKCPNGDCIS DSLLCNGIND CNDGSDEVHC LSNVTTHLVN
CSLNEYRCLG TDICLPKNVR CDGKNDCPQS DDEQNCTYCF ENEFACDNKR CIPELWVCDK
ANDCGDNSDE KNCDGSKRNF IESNECDEFK CSVGTCLPYS KVCDGNRDCP DGSDETGKCQ
TACTVNNFCK GMCYKTPAGA VCGCQSGYRL AVDMISCEDI NECELDICSQ MCRNTIGSYE
CFCKDEFIIR NDKTSCKAVG PAMEFITVTD NDIRKMTHNL HSTTQLLFPL MGVRVSGLDV
NAVSDSVYWS NDEFGTIKKL NIRTNEIVTV KIVEHPQALA VDWITGNVYV NDNSHLNTIK
VCNLEKGKCA TLVKIQDKMK VASVIVDSIN RWLFWAEISL EADHPTSKIC RTDMTGADMK
IIASDLGFVR GMTIDHVKSK LYWSDDFYKT VESSNFDGSQ RKVVLTLNMN HALSISIFEQ
SLYFLSSDNL LSSCKMYGKR SCEHVNIGAN NVFRLFSILH ISRQVPFANP CDAEYCDYMC
VLKKENATCI CSDGESIESN STCNIKNDLK FVESINFSRN TRNISGIYSI TIIVLLVSVL
LLCVYYYYQK NKLKSKPASN LSCSSIHFQN PSYDRSDEIE VMLDSMASSE LSPGQHEYIN
PINNKGMKAA ENNAKKSNQC SEGKNIEEEK QDALIYFVHN SK