ZNF22_MOUSE
ID ZNF22_MOUSE Reviewed; 237 AA.
AC Q9ERU3; Q3TF83; Q8VEK7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein 22;
DE AltName: Full=Zinc finger protein 422;
DE AltName: Full=Zinc finger protein Krox-25;
DE AltName: Full=Zinc finger protein Krox-26;
GN Name=Znf22; Synonyms=Krox25, Krox26, Zfp422;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAG12466.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAG12466.1};
RC TISSUE=Craniofacial {ECO:0000269|PubMed:14706453};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12489153; DOI=10.1080/03008200290001212;
RA Ganss B., Teo W., Chen H., Poon T.;
RT "Krox-26 is a novel C2H2 zinc finger transcription factor expressed in
RT developing dental and osteogenic tissues.";
RL Connect. Tissue Res. 43:161-166(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland {ECO:0000269|PubMed:15489334};
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).
RN [5] {ECO:0000305}
RP DNA-BINDING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12952191; DOI=10.1080/713713594;
RA Teo W., Chen H., Poon T., Ganss B.;
RT "Developmental expression pattern and DNA-binding properties of the zinc
RT finger transcription factor Krox-26.";
RL Connect. Tissue Res. 44:161-166(2003).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-23, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. {ECO:0000269|PubMed:12952191, ECO:0000303|PubMed:12489153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in developing craniofacial
CC bones and dental organs, and in molar tooth germs of postnatal animals.
CC Also detected in embryonic heart, liver, thymus, kidney, brain, lung,
CC muscle and calvaria. In the adult, highly expressed in lung, kidney,
CC bone and incisors. {ECO:0000269|PubMed:12489153,
CC ECO:0000269|PubMed:12952191, ECO:0000269|PubMed:14706453}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression is detected from day 7
CC with highest levels between days 11 and 15.
CC {ECO:0000269|PubMed:12489153, ECO:0000269|PubMed:12952191}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG12466.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF281634; AAG12466.1; ALT_FRAME; mRNA.
DR EMBL; AK082970; BAC38716.1; -; mRNA.
DR EMBL; AK169251; BAE41015.1; -; mRNA.
DR EMBL; BC018339; AAH18339.1; -; mRNA.
DR CCDS; CCDS20459.1; -.
DR RefSeq; NP_001289368.1; NM_001302439.1.
DR RefSeq; NP_001289369.1; NM_001302440.1.
DR RefSeq; NP_080333.1; NM_026057.3.
DR AlphaFoldDB; Q9ERU3; -.
DR SMR; Q9ERU3; -.
DR BioGRID; 212050; 1.
DR STRING; 10090.ENSMUSP00000078685; -.
DR iPTMnet; Q9ERU3; -.
DR PhosphoSitePlus; Q9ERU3; -.
DR EPD; Q9ERU3; -.
DR MaxQB; Q9ERU3; -.
DR PaxDb; Q9ERU3; -.
DR PRIDE; Q9ERU3; -.
DR ProteomicsDB; 275040; -.
DR Antibodypedia; 13486; 72 antibodies from 19 providers.
DR DNASU; 67255; -.
DR Ensembl; ENSMUST00000057540; ENSMUSP00000084926; ENSMUSG00000059878.
DR Ensembl; ENSMUST00000079749; ENSMUSP00000078685; ENSMUSG00000059878.
DR Ensembl; ENSMUST00000112880; ENSMUSP00000108501; ENSMUSG00000059878.
DR GeneID; 67255; -.
DR KEGG; mmu:67255; -.
DR UCSC; uc009dkj.1; mouse.
DR CTD; 67255; -.
DR MGI; MGI:1914505; Zfp422.
DR VEuPathDB; HostDB:ENSMUSG00000059878; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT01050000244959; -.
DR HOGENOM; CLU_002678_21_0_1; -.
DR InParanoid; Q9ERU3; -.
DR OMA; QKWGVTI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9ERU3; -.
DR TreeFam; TF350836; -.
DR BioGRID-ORCS; 67255; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Zfp422; mouse.
DR PRO; PR:Q9ERU3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9ERU3; protein.
DR Bgee; ENSMUSG00000059878; Expressed in ventricular zone and 76 other tissues.
DR Genevisible; Q9ERU3; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0042476; P:odontogenesis; NAS:UniProtKB.
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; 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 1: Evidence at protein 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_0000047349"
FT ZN_FING 55..77
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT ZN_FING 83..105
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT ZN_FING 111..133
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT ZN_FING 139..161
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT ZN_FING 167..189
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 192
FT /note="K -> N (in Ref. 1; AAG12466)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="R -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Q -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..237
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 27294 MW; 1653220411F3C7DD CRC64;
MRLGKPKGGI SRSASQGKAY ESKRKTARQR QKWGVAIRFD SGLSRRRRNV DEKPYKCAKC
SKSFSQSSTL FQHKKIHTGK KSHKCADCGK SFFQSSNLIQ HRRIHTGEKP YKCDECGERF
KQSSNLIQHQ RIHTGEKPYC CDECGRCFSQ SSHLIQHQRT HTGEKPYQCE ECDKCFSQSS
HLRQHMKVHK EKKPHKRGKN ARVKTHPVSW KRGKGRKAVA GIRQVKGATS GLFKKKK
