ID KRUP_TRICA Reviewed; 74 AA. AC Q01793; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 29-MAY-2024, entry version 106. DE RecName: Full=Protein krueppel; DE Flags: Fragment; GN Name=Kr; OS Tribolium castaneum (Red flour beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia; OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium. OX NCBI_TaxID=7070; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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). CC -!- FUNCTION: Krueppel is a gap class segmentation protein. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L01616; AAA30096.1; -; Genomic_DNA. DR AlphaFoldDB; Q01793; -. DR SMR; Q01793; -. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_056241_0_0_1; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter. DR GO; GO:0035282; P:segmentation; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR16515:SF46; FINGER PROTEIN, PUTATIVE-RELATED; 1. DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 2. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. PE 3: Inferred from homology; KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus; KW Repeat; Zinc; Zinc-finger. FT CHAIN <1..>74 FT /note="Protein krueppel" FT /id="PRO_0000047002" FT ZN_FING <1..4 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 10..32 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 38..60 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 66..>74 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT NON_TER 1 FT NON_TER 74 SQ SEQUENCE 74 AA; 9065 MW; 902C9B81C8D469DA CRC64; ERTHTGEKPF ECQECHKRFT RDHHLKTHMR LHTGERPYRC EHCDRQFVQV ANLRRHLRVH TGERPYGCEH CSMK //