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 11-DEC-2019, entry version 137. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAG12467.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP 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., Kozak C., RA Yamada Y.; RT "Molecular cloning, chromosomal mapping, and characteristic expression in RT 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Binds DNA through the consensus sequence 5'-CAATG-3'. May be CC involved in transcriptional regulation and may play a role in tooth CC formation (By similarity). {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 and CC thymus. {ECO:0000269|PubMed:14706453}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in presecretory ameloblasts with CC very high expression in secretory ameloblasts. Expression decreases in CC the maturation stage and is very low in the late maturation stage. CC {ECO:0000269|PubMed:14706453}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG12467.1; Type=Frameshift; 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_006237187.3. DR RefSeq; XP_006237251.1; XM_006237189.3. DR RefSeq; XP_006237252.1; XM_006237190.3. DR RefSeq; XP_008761471.1; XM_008763249.1. DR SMR; Q9ERU2; -. DR STRING; 10116.ENSRNOP00000018050; -. DR iPTMnet; Q9ERU2; -. DR PhosphoSitePlus; Q9ERU2; -. DR PaxDb; Q9ERU2; -. 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; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. DR GeneTree; ENSGT00980000198545; -. DR HOGENOM; HOG000234617; -. DR InParanoid; Q9ERU2; -. DR OMA; SWKAGKG; -. DR OrthoDB; 1318335at2759; -. DR PhylomeDB; Q9ERU2; -. DR TreeFam; TF350836; -. DR PRO; PR:Q9ERU2; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000013379; Expressed in 9 organ(s), highest expression level in liver. DR Genevisible; Q9ERU2; RN. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. 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 InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR Pfam; PF00096; zf-C2H2; 5. DR SMART; SM00355; ZnF_C2H2; 5. DR SUPFAM; SSF57667; SSF57667; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. PE 2: Evidence at transcript level; KW Acetylation; DNA-binding; Metal-binding; Nucleus; Reference proteome; KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..237 FT /note="Zinc finger protein 22" FT /id="PRO_0000047350" FT ZN_FING 55..82 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 83..110 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 111..138 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 139..166 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 167..194 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT MOD_RES 18 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9ERU3" FT MOD_RES 23 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9ERU3" FT CONFLICT 6 FT /note="P -> PQ (in Ref. 1; AAG12467)" FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="S -> T (in Ref. 1; AAG12467)" FT /evidence="ECO:0000305" FT CONFLICT 23 FT /note="K -> R (in Ref. 1; AAG12467)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="C -> Y (in Ref. 1; AAG12467)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="S -> N (in Ref. 1; AAG12467)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="K -> Q (in Ref. 1; AAG12467)" FT /evidence="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 //