ID KRUP_DROME STANDARD; PRT; 502 AA. AC P07247; Q8SYW3; Q9W0V9; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 16-MAY-2006, entry version 62. DE Protein krueppel. GN Name=Kr; ORFNames=CG3340; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE. RA Rosenberg U.B., Schroeder C., Preiss A., Kienlin A., Cote S., RA Riede I., Jaeckle H.; RT "Structural homology of the product of the Drosophila Krueppel gene RT with Xenopus transcription factor IIIA."; RL Nature 319:336-339(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., 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 MEDLINE=93066327; PubMed=1438276; RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.; RT "Evolutionary conservation pattern of zinc-finger domains of RT Drosophila segmentation genes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992). RN [6] RP SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION. RX MEDLINE=87289672; PubMed=3112773; 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). CC -!- FUNCTION: Krueppel is a gap class segmentation protein. It is CC involved in the segmentation of the embryo and in the CC differentiation of the Malpighian tubules. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromatin associated. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers. CC -!- CAUTION: Ref.1 sequence differs from that shown due to a CC frameshift in position 411. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03414; CAA27148.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE003466; AAF47321.1; -; Genomic_DNA. DR EMBL; AY071280; AAL48902.1; -; mRNA. DR PIR; A24566; TWFF. DR UniGene; Dm.2786; -. DR HSSP; P08047; 1SP2. DR TRANSFAC; T00456; -. DR Ensembl; CG3340; Drosophila melanogaster. DR FlyBase; FBgn0001325; Kr. DR GO; GO:0003677; F:DNA binding; IDA. DR GO; GO:0016564; F:transcriptional repressor activity; IDA. DR GO; GO:0007411; P:axon guidance; IMP. DR GO; GO:0007456; P:eye development (sensu Endopterygota); IMP. DR GO; GO:0007402; P:ganglion mother cell fate determination; TAS. DR GO; GO:0007443; P:Malpighian tubule morphogenesis; TAS. DR GO; GO:0007517; P:muscle development; TAS. DR GO; GO:0007400; P:neuroblast fate determination; IEP. DR GO; GO:0040034; P:regulation of development, heterochronic; TAS. DR GO; GO:0007419; P:ventral cord development; NAS. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 4. DR ProDom; PD000003; Znf_C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. KW Complete proteome; Developmental protein; DNA-binding; Gap protein; KW Metal-binding; Nuclear protein; Phosphorylation; Repeat; Zinc; KW Zinc-finger. FT CHAIN 1 502 Protein krueppel. FT /FTId=PRO_0000046992. FT ZN_FING 222 244 C2H2-type 1. FT ZN_FING 250 272 C2H2-type 2. FT ZN_FING 278 300 C2H2-type 3. FT ZN_FING 306 328 C2H2-type 4. FT ZN_FING 334 354 C2H2-type 5. FT CONFLICT 153 154 HE -> Q (in Ref. 4). FT CONFLICT 181 182 HT -> LS (in Ref. 1). FT CONFLICT 256 256 H -> D (in Ref. 1). FT CONFLICT 329 329 N -> T (in Ref. 1). FT CONFLICT 397 397 G -> S (in Ref. 1). FT CONFLICT 429 429 C -> Y (in Ref. 1). 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 //