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ECR_AEDAE
ID   ECR_AEDAE               Reviewed;         776 AA.
AC   P49880; Q16VE1; Q6VA69;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Ecdysone receptor;
DE   AltName: Full=20-hydroxy-ecdysone receptor;
DE            Short=20E receptor;
DE   AltName: Full=EcRH;
DE            Short=AaEcR;
DE   AltName: Full=Ecdysteroid receptor;
DE   AltName: Full=Nuclear receptor subfamily 1 group H member 1;
GN   Name=EcR; Synonyms=NR1H1; ORFNames=AAEL009600;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fat body;
RX   PubMed=7711747; DOI=10.1016/0965-1748(94)00045-j;
RA   Cho W.-L., Kapitskaya M.Z., Raikhel A.S.;
RT   "Mosquito ecdysteroid receptor: analysis of the cDNA and expression during
RT   vitellogenesis.";
RL   Insect Biochem. Mol. Biol. 25:19-27(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ALTERNATIVE SPLICING, DNA-BINDING,
RP   INTERACTION WITH USP, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12385823; DOI=10.1016/s0303-7207(02)00225-3;
RA   Wang S.-F., Li C., Sun G., Zhu J., Raikhel A.S.;
RT   "Differential expression and regulation by 20-hydroxyecdysone of mosquito
RT   ecdysteroid receptor isoforms A and B.";
RL   Mol. Cell. Endocrinol. 196:29-42(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
CC   -!- FUNCTION: Receptor for ecdysone. Binds to ecdysone response elements
CC       (ECRES). {ECO:0000269|PubMed:7711747}.
CC   -!- SUBUNIT: Heterodimer of USP and ECR. Only the heterodimer is capable of
CC       high-affinity binding to ecdysone. {ECO:0000269|PubMed:7711747}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P49880-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P49880-2; Sequence=VSP_035029;
CC   -!- TISSUE SPECIFICITY: A peak level expression is seen in the fat body of
CC       previtellogenic female mosquitos at one and two days after eclosion,
CC       levels fall three-fold at three days posteclosion.
CC       {ECO:0000269|PubMed:12385823, ECO:0000269|PubMed:7711747}.
CC   -!- INDUCTION: Transcripts exhibit dramatically different patterns of
CC       expression after blood meal-triggered activation of vitellogenesis in
CC       the fat body. Isoform B is highly expressed and reaches its peak at 4
CC       hours pbm (post blood meal). Isoform A peaks at 16-20 hours, when
CC       isoform B expression is lowest. {ECO:0000269|PubMed:12385823}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT38529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U02021; AAA87394.1; -; mRNA.
DR   EMBL; AY345989; AAQ23183.1; -; mRNA.
DR   EMBL; CH477596; EAT38529.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH477685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_001660279.1; XM_001660229.2.
DR   AlphaFoldDB; P49880; -.
DR   SMR; P49880; -.
DR   STRING; 7159.AAEL009600-PA; -.
DR   BindingDB; P49880; -.
DR   ChEMBL; CHEMBL3413; -.
DR   VEuPathDB; VectorBase:AAEL019431; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   HOGENOM; CLU_007368_12_4_1; -.
DR   InParanoid; P49880; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035100; F:ecdysone binding; IEA:InterPro.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd06938; NR_LBD_EcR; 1.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR003069; Ecdystd_rcpt.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR041889; NR_LBD_EcR.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01283; ECDYSTEROIDR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..776
FT                   /note="Ecdysone receptor"
FT                   /id="PRO_0000053525"
FT   DOMAIN          437..673
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        288..363
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         291..311
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         327..346
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..290
FT                   /note="Modulating"
FT                   /evidence="ECO:0000255"
FT   REGION          199..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..255
FT                   /note="MYRLNIVSTNPSGSVQQQQQAQGQQVISSVVRPQQQQPPPQLALVQTGGSGG
FT                   TTTTIIGLTSLNALNATTITGLVAGAAGSSTSAIAAAGASNSGSGPSTATTKHILKAAT
FT                   TNNNISIVKIVDDIMLKAVKVEPLPMDTGGGGGGVSMIPSSATTSGGVTVTAIPASVAP
FT                   MPPVAAGTNVSSNGSVTVYASGKRRLESNEEWISSPSPGSVPGSAPPLSPSPGSQSTTY
FT                   TTTMSNGYSSPMSTGSYDPYSPNGKM -> MMKRRWSNNGGFTALRMLDDSSSEVTSSS
FT                   AALGMTMSPNSLGSPNYDELELWSSYEDNAYNGHSVLSNGNNNLGGCGAANNLLMNGIV
FT                   GNNNLNGMMNMASQAVQANANSIQHIVGNLINGVNPNQTLIPPLPSIIQNTLMNTPRSE
FT                   SVNSISSAALGMTMSPNSLGSPNYDELELWSSYEDNAYNGHSVLSNG (in isoform
FT                   B)"
FT                   /evidence="ECO:0000303|PubMed:7711747"
FT                   /id="VSP_035029"
SQ   SEQUENCE   776 AA;  83645 MW;  C9B1E893C08E0CAC CRC64;
     MYRLNIVSTN PSGSVQQQQQ AQGQQVISSV VRPQQQQPPP QLALVQTGGS GGTTTTIIGL
     TSLNALNATT ITGLVAGAAG SSTSAIAAAG ASNSGSGPST ATTKHILKAA TTNNNISIVK
     IVDDIMLKAV KVEPLPMDTG GGGGGVSMIP SSATTSGGVT VTAIPASVAP MPPVAAGTNV
     SSNGSVTVYA SGKRRLESNE EWISSPSPGS VPGSAPPLSP SPGSQSTTYT TTMSNGYSSP
     MSTGSYDPYS PNGKMGREDL SPSSSLNGYT DGSDAKKQKK GPTPRQQEEL CLVCGDRESG
     YHYNALTCEG CKGFFRRSVT KNAVYCCKFG HACEMDMYMR RKCQECRLKK CLAVGMRPEC
     VVPENQCAIK RKEKKAQKEK DKVQTNATVS TTNSTYRSEI LPILMKCDPP PHQAIPLLPE
     KLLQENRLRN IPLLTANQMA VIYKLIWYQD GYEQPSEEDL KRIMIGSPNE EEDQHDVHFR
     HITEITILTV QLIVEFAKGL PAFTKIPQED QITLLKACSS EVMMLRMARR YDAATDSILF
     ANNRSYTRDS YRMAGMADTI EDLLHFCRQM FSLTVDNVEY ALLTAIVIFS DRPGLEQAEL
     VEHIQSYYID TLRIYILNRH AGDPKCSVIF AKLLSILTEL RTLGNQNSEM CFSLKLKNRK
     LPRFLEEIWD VQDIPPSMQA QMHSHGTQSS SSSSSSSSSS SNGSSNGNSS SNSNSSQHGP
     HPHPHGQQLT PNQQQHQQQH SQLQQVHANG SGSGGGSNNN SSSGGVVPGL GMLDQV
 
 
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