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KRH1_DROME
ID   KRH1_DROME              Reviewed;         845 AA.
AC   P08155; Q9VMH5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Krueppel homolog 1;
DE   AltName: Full=Krueppel homologous protein 1;
GN   Name=Kr-h1; Synonyms=Kr-h; ORFNames=CG9167;
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 [MRNA] (ISOFORMS ALPHA AND BETA), FUNCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R; TISSUE=Embryo, Larva, and Pupae;
RX   PubMed=10772791; DOI=10.1006/dbio.2000.9687;
RA   Pecasse F., Beck Y., Ruiz C., Richards G.;
RT   "Kruppel-homolog, a stage-specific modulator of the prepupal ecdysone
RT   response, is essential for Drosophila metamorphosis.";
RL   Dev. Biol. 221:53-67(2000).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM BETA).
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 [MRNA] OF 289-367.
RX   PubMed=3096579; DOI=10.1016/0092-8674(86)90817-2;
RA   Schuh R., Aicher W., Gaul U., Cote S., Preiss A., Maier D., Seifert E.,
RA   Nauber U., Schroeder C., Kemler R., Jaeckle H.;
RT   "A conserved family of nuclear proteins containing structural elements of
RT   the finger protein encoded by Kruppel, a Drosophila segmentation gene.";
RL   Cell 47:1025-1032(1986).
CC   -!- FUNCTION: Plays a general role in the hierarchies of gene expression
CC       leading to metamorphosis. {ECO:0000269|PubMed:10772791}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta;
CC         IsoId=P08155-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=P08155-2; Sequence=VSP_006830;
CC   -!- DEVELOPMENTAL STAGE: Beta isoform is expressed during embryogenesis,
CC       most abundant in midembryogenesis, and in adults. Alpha isoform is
CC       expressed from embryogenesis to 8 hours after pupariation, major period
CC       of expression is during second instar. {ECO:0000269|PubMed:10772791}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ005440; CAA06543.2; -; mRNA.
DR   EMBL; AJ005441; CAA06544.2; -; mRNA.
DR   EMBL; AE014134; AAF52343.2; -; Genomic_DNA.
DR   EMBL; AE014134; AAG22417.1; -; Genomic_DNA.
DR   EMBL; AY051816; AAK93240.1; -; mRNA.
DR   EMBL; M14940; AAA28660.1; -; mRNA.
DR   RefSeq; NP_477466.1; NM_058118.5. [P08155-1]
DR   RefSeq; NP_477467.1; NM_058119.5. [P08155-2]
DR   AlphaFoldDB; P08155; -.
DR   SMR; P08155; -.
DR   BioGRID; 60025; 13.
DR   IntAct; P08155; 11.
DR   STRING; 7227.FBpp0288736; -.
DR   PaxDb; P08155; -.
DR   PRIDE; P08155; -.
DR   EnsemblMetazoa; FBtr0344437; FBpp0310809; FBgn0266450. [P08155-2]
DR   EnsemblMetazoa; FBtr0344438; FBpp0310810; FBgn0266450. [P08155-1]
DR   GeneID; 33861; -.
DR   KEGG; dme:Dmel_CG45074; -.
DR   CTD; 33861; -.
DR   FlyBase; FBgn0266450; Kr-h1.
DR   VEuPathDB; VectorBase:FBgn0266450; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_014679_0_1_1; -.
DR   InParanoid; P08155; -.
DR   PhylomeDB; P08155; -.
DR   BioGRID-ORCS; 33861; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Kr-h1; fly.
DR   GenomeRNAi; 33861; -.
DR   PRO; PR:P08155; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0266450; Expressed in brain and 36 other tissues.
DR   Genevisible; P08155; DM.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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:0007552; P:metamorphosis; IMP:FlyBase.
DR   GO; GO:0045316; P:negative regulation of compound eye photoreceptor development; IMP:FlyBase.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IGI: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; ISS:FlyBase.
DR   GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
DR   GO; GO:0042594; P:response to starvation; IDA:FlyBase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..845
FT                   /note="Krueppel homolog 1"
FT                   /id="PRO_0000046991"
FT   ZN_FING         194..216
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..407
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         413..435
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         441..463
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          141..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..54
FT                   /note="Missing (in isoform Alpha)"
FT                   /evidence="ECO:0000303|PubMed:10772791"
FT                   /id="VSP_006830"
FT   CONFLICT        313
FT                   /note="N -> D (in Ref. 5; AAA28660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   845 AA;  91452 MW;  A4D878E98DC8E372 CRC64;
     MTESKNDTKS WAPKQIWIKD VLKKSGTELL DISKSPAKAV AVKKSPAKDS ATTKMVYYSA
     NQLLIKTEQS SQAQFCLQVP PPLTATTTSV GLGVPPSGGQ QEHFELLQTP QQRQMQLQLQ
     DQHQQEQQQF VSYQLAIQQH QKQQQQQQHE SITNAAPTAA PSAQRIKTEP VGGFPASAAV
     VSQVRKPSAS KPQFKCDQCG MTFGSKSAHT SHTKSHSKNQ DLSLNGASGA GVAAPVSTAA
     IELNDAGLPV GIPKSPTIKP LANVAAGADP YQCNVCQKTF AVPARLIRHY RTHTGERPFE
     CEFCHKLFSV KENLQVHRRI HTKERPYKCD VCGRAFEHSG KLHRHMRIHT GERPHKCSVC
     EKTFIQSGQL VIHMRTHTGE KPYKCPEPGC GKGFTCSKQL KVHSRTHTGE KPYHCDICFR
     DFGYNHVLKL HRVQHYGSKC YKCTICDETF KNKKEMEAHI KGHANEVPDD EAEAAAASAA
     ASTSAGSSAG SPSLQGVSSN SESSNHSPPS SPPATKKPRQ ARQPRVSKTV AATLSIPTSS
     PLSPSSLSST YSPSASSMAS PPPTSAHYLP VQMEADALSR DSGVSSAQPA HSTYADEEPT
     DLSMQQVQGQ LPESTVDYYQ APPSLLELQP QPAGLTINPA LLEAASIARR HDDNDDQVQD
     EDVHAAAWQM MQLCRGHGSL PPTEQPAPSH QPQVPTLHVS DLAANYDDTH EATVLIEHFK
     RGDLARHGLH KGYAPVPKYE SALPNPDVVR RVEAAIGLRS STESPERSSS PESDSLMMAD
     RNVMTLPLRK RKHYMNKGDD GQVDSEKASG DGTSAAGGAA SVGAGDGPGS KVMRMSSVIQ
     FAKAS
 
 
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