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Database: UniProt
Entry: Q6X0I2
LinkDB: Q6X0I2
Original site: Q6X0I2 
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   16-JAN-2019, entry version 78.
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;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Myrmicinae; Solenopsis.
OX   NCBI_TaxID=13686;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAP92450.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL 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
RT   receptor from the imported fire ant, Solenopsis invicta Buren
RT   (Hymenoptera: Formicidae).";
RL   Insect Mol. Biol. 13:195-204(2004).
CC   -!- FUNCTION: Involved in uptake of vitellogenin by endocytosis.
CC       Expression is regulated by the juvenile hormone analog, methoprene
CC       (in vitro). {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
CC       the previtellogenic period in virgin alate females, then decrease
CC       in reproductive females. {ECO:0000269|PubMed:15056367}.
DR   EMBL; AY262832; AAP92450.1; -; mRNA.
DR   RefSeq; NP_001291525.1; NM_001304596.1.
DR   ProteinModelPortal; Q6X0I2; -.
DR   PRIDE; Q6X0I2; -.
DR   GeneID; 105200757; -.
DR   KEGG; soc:105200757; -.
DR   OrthoDB; 340714at2759; -.
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   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; 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;
KW   Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1782       Vitellogenin receptor. {ECO:0000255}.
FT                                /FTId=PRO_0000378058.
FT   TOPO_DOM     19   1663       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1664   1684       Helical. {ECO:0000255}.
FT   TOPO_DOM   1685   1782       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       35     72       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       81    118       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      122    157       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      166    205       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      208    243       EGF-like 1. {ECO:0000255}.
FT   DOMAIN      244    283       EGF-like; calcium-binding. {ECO:0000255}.
FT   REPEAT      327    374       LDL-receptor class B 1. {ECO:0000255}.
FT   REPEAT      375    416       LDL-receptor class B 2. {ECO:0000255}.
FT   REPEAT      417    460       LDL-receptor class B 3. {ECO:0000255}.
FT   REPEAT      461    501       LDL-receptor class B 4. {ECO:0000255}.
FT   REPEAT      502    544       LDL-receptor class B 5. {ECO:0000255}.
FT   DOMAIN      552    588       EGF-like 2. {ECO:0000255}.
FT   DOMAIN      889    927       EGF-like 3. {ECO:0000255}.
FT   DOMAIN      931    969       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      973   1009       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1012   1049       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1052   1090       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1094   1131       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1140   1177       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1178   1214       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1225   1260       LDL-receptor class A 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1262   1298       EGF-like 4. {ECO:0000255}.
FT   REPEAT     1385   1425       LDL-receptor class B 6. {ECO:0000255}.
FT   REPEAT     1471   1518       LDL-receptor class B 7. {ECO:0000255}.
FT   REPEAT     1519   1561       LDL-receptor class B 8. {ECO:0000255}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    159    159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    239    239       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    702    702       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    859    859       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    896    896       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    923    923       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1133   1133       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1140   1140       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1175   1175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1626   1626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1640   1640       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1656   1656       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     36     48       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     43     61       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     55     71       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     82     94       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     89    107       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    101    117       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    123    134       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    129    147       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    141    156       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    167    181       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    176    194       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    188    204       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    248    258       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    254    267       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    269    282       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    932    945       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    939    958       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    952    968       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    974    986       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    981    999       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    993   1008       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1013   1026       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1020   1039       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1033   1048       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1053   1065       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1060   1078       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1072   1089       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1095   1108       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1103   1121       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1115   1130       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1141   1154       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1148   1167       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1161   1176       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1179   1191       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1186   1204       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1198   1213       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1226   1236       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1231   1249       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1243   1259       {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
//
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