KRUP_DROME
ID KRUP_DROME Reviewed; 502 AA.
AC P07247; Q8SYW3; Q9W0V9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein krueppel;
GN Name=Kr; ORFNames=CG3340;
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].
RA Rosenberg U.B., Schroeder C., Preiss A., Kienlin A., Cote S., Riede I.,
RA Jaeckle H.;
RT "Structural homology of the product of the Drosophila Krueppel gene with
RT Xenopus transcription factor IIIA.";
RL Nature 319:336-339(1986).
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=Embryo;
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 NUCLEOTIDE SEQUENCE OF 240-314.
RX PubMed=1438276; DOI=10.1073/pnas.89.22.10782;
RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.;
RT "Evolutionary conservation pattern of zinc-finger domains of Drosophila
RT segmentation genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992).
RN [6]
RP SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION.
RX PubMed=3112773; DOI=10.1073/pnas.84.16.5700;
RA Ollo R., Maniatis T.;
RT "Drosophila Kruppel gene product produced in a baculovirus expression
RT system is a nuclear phosphoprotein that binds to DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5700-5704(1987).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-471 AND SER-477, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Krueppel is a gap class segmentation protein. It is involved
CC in the segmentation of the embryo and in the differentiation of the
CC Malpighian tubules.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3112773}.
CC Note=Chromatin associated.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27148.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X03414; CAA27148.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE013599; AAF47321.1; -; Genomic_DNA.
DR EMBL; AY071280; AAL48902.1; -; mRNA.
DR PIR; A24566; TWFF.
DR RefSeq; NP_001261181.1; NM_001274252.1.
DR RefSeq; NP_523867.1; NM_079143.3.
DR AlphaFoldDB; P07247; -.
DR SMR; P07247; -.
DR BioGRID; 63578; 42.
DR IntAct; P07247; 4.
DR STRING; 7227.FBpp0305365; -.
DR iPTMnet; P07247; -.
DR PaxDb; P07247; -.
DR EnsemblMetazoa; FBtr0072449; FBpp0072351; FBgn0001325.
DR EnsemblMetazoa; FBtr0333162; FBpp0305365; FBgn0001325.
DR GeneID; 38012; -.
DR KEGG; dme:Dmel_CG3340; -.
DR CTD; 38012; -.
DR FlyBase; FBgn0001325; Kr.
DR VEuPathDB; VectorBase:FBgn0001325; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_030522_1_0_1; -.
DR InParanoid; P07247; -.
DR OMA; SDMPEQT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P07247; -.
DR SignaLink; P07247; -.
DR BioGRID-ORCS; 38012; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38012; -.
DR PRO; PR:P07247; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001325; Expressed in anlage in statu nascendi and 46 other tissues.
DR ExpressionAtlas; P07247; baseline and differential.
DR Genevisible; P07247; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0061332; P:Malpighian tubule bud morphogenesis; IGI:FlyBase.
DR GO; GO:0007517; P:muscle organ development; TAS:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; TAS:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:FlyBase.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; TAS:FlyBase.
DR InterPro; IPR031243; Krueppel.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24390:SF151; PTHR24390:SF151; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..502
FT /note="Protein krueppel"
FT /id="PRO_0000046992"
FT ZN_FING 222..244
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..354
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 115..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 153..154
FT /note="HE -> Q (in Ref. 4; AAL48902)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="HT -> LS (in Ref. 1; CAA27148)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="H -> D (in Ref. 1; CAA27148)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="N -> T (in Ref. 1; CAA27148)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="G -> S (in Ref. 1; CAA27148)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="C -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54715 MW; 67A94177A701D976 CRC64;
MSISMLQDAQ TRTLAAALAG IKQEDVHLDR SMSLSPPMSA NTSATSAAAI YPAMGLQQAA
AASAFGMLSP TQLLAANRQA AAFMAQLPMS TLANTLFPHN PAALFGAWAA QQSLPPQGTH
LHSPPASPHS PLSTPLGSGK HPLNSPNSTP QHHEPAKKAR KLSVKKEFQT EISMSVNDMY
HTSGGPISPP SSGSSPNSTH DGAGGNAGCV GVSKDPSRDK SFTCKICSRS FGYKHVLQNH
ERTHTGEKPF ECPECHKRFT RDHHLKTHMR LHTGEKPYHC SHCDRQFVQV ANLRRHLRVH
TGERPYTCEI CDGKFSDSNQ LKSHMLVHNG EKPFECERCH MKFRRRHHLM NHKCGIQSPP
TPALSPAMSG DYPVAISAIA IEASTNRFAA MCATYGGSNE SVDMEKATPE DDGPLDLSED
GASSVDGHCS NIARRKAQDI RRVFRLPPPQ IPHVPSDMPE QTEPEDLSMH SPRSIGSHEQ
TDDIDLYDLD DAPASYMGHQ QH
