ZN260_MOUSE
ID ZN260_MOUSE Reviewed; 407 AA.
AC Q62513; Q3U170; Q8C2Q6; Q9R2B4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger protein 260;
DE Short=Zfp-260;
GN Name=Znf260; Synonyms=Zfp260;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=10449921; DOI=10.1159/000015316;
RA Blottiere L., Apiou F., Ferbus D., Guenzi C., Dutrillaux B.,
RA Prosperi M.-T., Goubin G.;
RT "Cloning, characterization, and chromosome assignment of Zfp146 the mouse
RT ortholog of human ZNF146, a gene amplified and overexpressed in pancreatic
RT cancer, and Zfp260 a closely related gene.";
RL Cytogenet. Cell Genet. 85:297-300(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Hippocampus;
RA Namikawa K., Morita N., Suzuki J., Kato K., Shiosaka S., Kiyama H.;
RT "Molecular cloning, brain localization, and ontogeny of a novel murine zinc
RT finger protein gene.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen, and Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16166646; DOI=10.1128/mcb.25.19.8669-8682.2005;
RA Debrus S., Rahbani L., Marttila M., Delorme B., Paradis P., Nemer M.;
RT "The zinc finger-only protein Zfp260 is a novel cardiac regulator and a
RT nuclear effector of alpha1-adrenergic signaling.";
RL Mol. Cell. Biol. 25:8669-8682(2005).
CC -!- FUNCTION: Transcription factor that acts as a cardiac regulator and an
CC effector of alpha1-adrenergic signaling. Binds to PE response elements
CC (PERE) present in the promoter of genes such as ANF/NPPA and acts as a
CC direct transcriptional activator of NPPA. Also acts as a cofactor with
CC GATA4, a key cardiac regulator.
CC -!- SUBUNIT: Binds DNA. Interacts with GATA4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly present in heart. Outside the heart,
CC it is detected in embryonic and postnatal vascular smooth muscle cells
CC and in epithelial cells of the lung, gut and kidney at sites of
CC epithelial morphogenesis and in the spinal cord (at protein level).
CC {ECO:0000269|PubMed:10449921, ECO:0000269|PubMed:16166646}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, it is predominantly detected in
CC cardiomyocyte nuclei This expression is maintained throughout embryonic
CC development in the atria and in the ventricular walls and trabeculae.
CC Also present in the outflow tract, the truncus arteriosus, the
CC developing atrioventricular valve and the cushion mesenchyme. Appears
CC to decrease after 14 dpc and by 17.5 dpc; it is then spatially
CC redistributed, with highest levels in subendocardial myocytes and the
CC septum and no expression in epicardial and apical myocytes. It is also
CC strongly expressed in the atrioventricular valve. During postnatal
CC development, it decreases in both atria and ventricles. In the adult
CC heart, expression is found in the aortic valve in scattered cells and
CC in the atria, ventricles, and septum. Interestingly, it is markedly up-
CC regulated in hypertrophied adult ventricles of transgenic mice
CC overexpressing the angiotensin II receptor (at protein level).
CC {ECO:0000269|PubMed:16166646}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AJ224805; CAB38535.1; -; Genomic_DNA.
DR EMBL; D45210; BAA08144.1; -; mRNA.
DR EMBL; AK088177; BAC40191.1; -; mRNA.
DR EMBL; AK156219; BAE33630.1; -; mRNA.
DR EMBL; BC082570; AAH82570.1; -; mRNA.
DR EMBL; BC085180; AAH85180.1; -; mRNA.
DR CCDS; CCDS21078.1; -.
DR RefSeq; NP_036111.2; NM_011981.4.
DR RefSeq; XP_011248885.1; XM_011250583.1.
DR RefSeq; XP_011248886.1; XM_011250584.2.
DR AlphaFoldDB; Q62513; -.
DR SMR; Q62513; -.
DR STRING; 10090.ENSMUSP00000052200; -.
DR iPTMnet; Q62513; -.
DR PhosphoSitePlus; Q62513; -.
DR EPD; Q62513; -.
DR MaxQB; Q62513; -.
DR PaxDb; Q62513; -.
DR PeptideAtlas; Q62513; -.
DR PRIDE; Q62513; -.
DR ProteomicsDB; 275005; -.
DR Antibodypedia; 48040; 48 antibodies from 11 providers.
DR DNASU; 26466; -.
DR Ensembl; ENSMUST00000050735; ENSMUSP00000052200; ENSMUSG00000049421.
DR Ensembl; ENSMUST00000108200; ENSMUSP00000103835; ENSMUSG00000049421.
DR GeneID; 26466; -.
DR KEGG; mmu:26466; -.
DR UCSC; uc009gde.1; mouse.
DR CTD; 26466; -.
DR MGI; MGI:1347071; Zfp260.
DR VEuPathDB; HostDB:ENSMUSG00000049421; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162468; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q62513; -.
DR OMA; FSQKSHY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q62513; -.
DR TreeFam; TF341817; -.
DR BioGRID-ORCS; 26466; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp260; mouse.
DR PRO; PR:Q62513; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62513; protein.
DR Bgee; ENSMUSG00000049421; Expressed in gonadal ridge and 257 other tissues.
DR ExpressionAtlas; Q62513; baseline and differential.
DR Genevisible; Q62513; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..407
FT /note="Zinc finger protein 260"
FT /id="PRO_0000047321"
FT ZN_FING 23..45
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 51..73
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 79..101
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 131..153
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 159..181
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..209
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="L -> H (in Ref. 3; BAE33630)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="R -> K (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> R (in Ref. 3; BAC40191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46443 MW; CC4076461018692A CRC64;
MLESLQPESH LLHDEPDPGE SVYECNECKE TFSLEQNFVE HKKTHSGEKS PECTGCGEES
SQASSLTLHL RSRPRRESYK CGECGKAFSQ RGNFLSHQKQ HTEERPSESK KTPVPMTTTV
RNQRNTGNKP YACKECGKAF NGKSYLKEHE KIHTGEKPFE CSQCGRAFSQ KQYLIKHQNI
HSGKKPFKCN ECGKAFSQKE NLIIHQRIHT GEKPYECKGC GKAFIQKSSL IRHQRSHTGE
KPYTCKECGK AFSGKSNLTE HEKIHIGEKP YKCNECGTIF RQKQYLIKHH NIHTGEKPYE
CNKCGKAFSR ITSLIVHVRI HTGDKPYECK ICGKAFCQSS SLTVHMRSHT GEKPYGCNEC
GKAFSQFSTL ALHMRIHTGE KPYQCSECGK AFSQKSHHIR HQRIHIH
