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KNIR_DROME
ID   KNIR_DROME              Reviewed;         429 AA.
AC   P10734; Q540X6; Q9VPC6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 194.
DE   RecName: Full=Zygotic gap protein knirps;
DE   AltName: Full=Nuclear receptor subfamily 0 group A member 1;
GN   Name=kni; Synonyms=NR0A1; ORFNames=CG4717;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R; TISSUE=Salivary gland;
RX   PubMed=2904128; DOI=10.1038/336489a0;
RA   Nauber U., Pankratz M.J., Kilnlin A., Seyffert E., Klemm U., Jackle H.;
RT   "Abdominal segmentation of the Drosophila embryo requires a hormone
RT   receptor-like protein encoded by the gap gene knirps.";
RL   Nature 336:489-492(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8670869; DOI=10.1002/j.1460-2075.1996.tb00735.x;
RA   Arnosti D.N., Gray S., Barolo S., Zhou J., Levine M.;
RT   "The gap protein knirps mediates both quenching and direct repression in
RT   the Drosophila embryo.";
RL   EMBO J. 15:3659-3666(1996).
CC   -!- FUNCTION: Transcriptional repressor. Binds to multiple sites in the eve
CC       stripe 3 enhancer element. Plays an essential role in the segmentation
CC       process both by refining the expression patterns of gap genes and by
CC       establishing pair-rules stripes of gene expression.
CC       {ECO:0000269|PubMed:8670869}.
CC   -!- INTERACTION:
CC       P10734; O46036: CtBP; NbExp=5; IntAct=EBI-170297, EBI-159330;
CC       P10734; P16371: gro; NbExp=5; IntAct=EBI-170297, EBI-153866;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC       ECO:0000269|PubMed:8670869}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR0
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X13331; CAA31709.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF51629.2; -; Genomic_DNA.
DR   EMBL; AY118798; AAM50658.1; -; mRNA.
DR   PIR; S01919; S01919.
DR   RefSeq; NP_524187.1; NM_079463.3.
DR   AlphaFoldDB; P10734; -.
DR   SMR; P10734; -.
DR   BioGRID; 65544; 30.
DR   DIP; DIP-17716N; -.
DR   ELM; P10734; -.
DR   IntAct; P10734; 11.
DR   MINT; P10734; -.
DR   STRING; 7227.FBpp0077941; -.
DR   PaxDb; P10734; -.
DR   DNASU; 40287; -.
DR   EnsemblMetazoa; FBtr0078283; FBpp0077941; FBgn0001320.
DR   GeneID; 40287; -.
DR   KEGG; dme:Dmel_CG4717; -.
DR   CTD; 40287; -.
DR   FlyBase; FBgn0001320; kni.
DR   VEuPathDB; VectorBase:FBgn0001320; -.
DR   eggNOG; ENOG502QURP; Eukaryota.
DR   GeneTree; ENSGT00940000170271; -.
DR   HOGENOM; CLU_633508_0_0_1; -.
DR   InParanoid; P10734; -.
DR   OrthoDB; 1136195at2759; -.
DR   PhylomeDB; P10734; -.
DR   Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-DME-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR   Reactome; R-DME-8939211; ESR-mediated signaling.
DR   Reactome; R-DME-8940973; RUNX2 regulates osteoblast differentiation.
DR   Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   SignaLink; P10734; -.
DR   BioGRID-ORCS; 40287; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 40287; -.
DR   PRO; PR:P10734; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0001320; Expressed in tracheal pit and 60 other tissues.
DR   ExpressionAtlas; P10734; baseline and differential.
DR   Genevisible; P10734; DM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007427; P:epithelial cell migration, open tracheal system; TAS:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR   GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; TAS:FlyBase.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..429
FT                   /note="Zygotic gap protein knirps"
FT                   /id="PRO_0000053743"
FT   DNA_BIND        2..78
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         5..25
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         42..66
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          112..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  45611 MW;  79CEE86A66AB00C7 CRC64;
     MNQTCKVCGE PAAGFHFGAF TCEGCKSFFG RSYNNISTIS ECKNEGKCII DKKNRTTCKA
     CRLRKCYNVG MSKGGSRYGR RSNWFKIHCL LQEHEQAAAA AGKAPPLAGG VSVGGAPSAS
     SPVGSPHTPG FGDMAAHLHH HHQQQQQQQV PRHPHMPLLG YPSYLSDPSA ALPFFSMMGG
     VPHQSPFQLP PHLLFPGYHA SAAAAAASAA DAAYRQEMYK HRQSVDSVES QNRFSPASQP
     PVVQPTSSAR QSPIDVCLEE DVHSVHSHQS SASLLHPIAI RATPTTPTSS SPLSFAAKMQ
     SLSPVSVCSI GGETTSVVPV HPPTVSAQEG PMDLSMKTSR SSVHSFNDSG SEDQEVEVAP
     RRKFYQLEAE CLTTSSSSSS HSAAHSPNTT TAHAEVKRQK LGGAEATHFG GFAVAHNAAS
     AMRGIFVCV
 
 
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