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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
 
 
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