ID ZNF22_RAT Reviewed; 237 AA. AC Q9ERU2; Q5EAN1; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 29-OCT-2014, entry version 99. DE RecName: Full=Zinc finger protein 22; DE AltName: Full=Zinc finger protein Krox-25; GN Name=Znf22; Synonyms=Krox25, Zfp422; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAG12467.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAG12467.1}; RX PubMed=14706453; DOI=10.1016/j.ygeno.2003.08.006; RA Lee S.K., Kim Y.S., Lee S.S., Lee Y.J., Song I.S., Park S.C., RA Kozak C., Yamada Y.; RT "Molecular cloning, chromosomal mapping, and characteristic expression RT in tooth organ of rat and mouse Krox-25."; RL Genomics 83:243-253(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Binds DNA through the consensus sequence 5'-CAATG-3'. CC May be involved in transcriptional regulation and may play a role CC in tooth formation (By similarity). CC {ECO:0000250|UniProtKB:Q9ERU3}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14706453}. CC -!- TISSUE SPECIFICITY: Highly expressed in the ameloblast layer of CC mandibular incisors, moderately expressed in submandibular gland, CC calvaria, kidney and lung, and expressed at low levels in brain CC and thymus. {ECO:0000269|PubMed:14706453}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in presecretory ameloblasts CC with very high expression in secretory ameloblasts. Expression CC decreases in the maturation stage and is very low in the late CC maturation stage. {ECO:0000269|PubMed:14706453}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00042, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG12467.1; Type=Frameshift; Positions=224; Evidence={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; AF281635; AAG12467.1; ALT_FRAME; mRNA. DR EMBL; BC090354; AAH90354.1; -; mRNA. DR RefSeq; NP_001012763.1; NM_001012745.1. DR RefSeq; XP_006237249.1; XM_006237187.2. DR RefSeq; XP_006237251.1; XM_006237189.2. DR RefSeq; XP_006237252.1; XM_006237190.2. DR UniGene; Rn.105961; -. DR ProteinModelPortal; Q9ERU2; -. DR SMR; Q9ERU2; 52-190. DR PRIDE; Q9ERU2; -. DR Ensembl; ENSRNOT00000018050; ENSRNOP00000018050; ENSRNOG00000013379. DR GeneID; 360389; -. DR KEGG; rno:360389; -. DR UCSC; RGD:620229; rat. DR CTD; 67255; -. DR RGD; 620229; Zfp422. DR eggNOG; COG5048; -. DR GeneTree; ENSGT00630000089829; -. DR HOGENOM; HOG000234617; -. DR HOVERGEN; HBG018163; -. DR InParanoid; Q9ERU2; -. DR OMA; THLVSSW; -. DR OrthoDB; EOG7QG44V; -. DR PhylomeDB; Q9ERU2; -. DR TreeFam; TF350836; -. DR NextBio; 672788; -. DR PRO; PR:Q9ERU2; -. DR Genevestigator; Q9ERU2; -. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042476; P:odontogenesis; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.60; -; 5. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Zinc; Zinc-finger. FT CHAIN 1 237 Zinc finger protein 22. FT /FTId=PRO_0000047350. FT ZN_FING 55 82 C2H2-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 83 110 C2H2-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 111 138 C2H2-type 3. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 139 166 C2H2-type 4. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 167 194 C2H2-type 5. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT MOD_RES 18 18 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 23 23 N6-acetyllysine. {ECO:0000250}. FT CONFLICT 6 6 P -> PQ (in Ref. 1; AAG12467). FT {ECO:0000305}. FT CONFLICT 15 15 S -> T (in Ref. 1; AAG12467). FT {ECO:0000305}. FT CONFLICT 23 23 K -> R (in Ref. 1; AAG12467). FT {ECO:0000305}. FT CONFLICT 140 140 C -> Y (in Ref. 1; AAG12467). FT {ECO:0000305}. FT CONFLICT 179 179 S -> N (in Ref. 1; AAG12467). FT {ECO:0000305}. FT CONFLICT 190 190 K -> Q (in Ref. 1; AAG12467). FT {ECO:0000305}. SQ SEQUENCE 237 AA; 27286 MW; 9945E6C00AEC6624 CRC64; MRLGKPKGGI SRSASQGKTY ESKRKTARQR QKWGVAIRFD SGLSRRRRNV DEKPYKCTKC SKSFSQSSTL FQHKKIHTGK KSHKCADCGK SFFQSSNLIQ HRRIHTGEKP YKCDECGERF KQSSNLIQHQ RIHTGEKPYC CDECGRCFSQ SSHLIQHQRT HTGEKPYQCE ECDKCFSQSS HLRQHMKVHK EKKSHKRGKN ARAKTHPVSW KRGKGRKAVA GLRQVKGAAS GLFKKKK //