ZN219_DANRE
ID ZN219_DANRE Reviewed; 1095 AA.
AC F1QQA8; S4TLP4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Zinc finger protein 219 {ECO:0000312|ZFIN:ZDB-GENE-110623-1};
DE AltName: Full=Zinc finger protein 219-like {ECO:0000303|PubMed:24155663};
GN Name=znf219 {ECO:0000312|ZFIN:ZDB-GENE-110623-1};
GN Synonyms=znf219l {ECO:0000303|PubMed:24155663};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:AGE89832.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=24155663; DOI=10.7150/ijbs.7126;
RA Lien H.W., Yang C.H., Cheng C.H., Hung C.C., Liao W.H., Hwang P.P.,
RA Han Y.S., Huang C.J.;
RT "A novel zinc finger protein 219-like (ZNF219L) is involved in the
RT regulation of collagen type 2 alpha 1a (col2a1a) gene expression in
RT zebrafish notochord.";
RL Int. J. Biol. Sci. 9:872-886(2013).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SOX9A, SUBCELLULAR LOCATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24269816; DOI=10.1016/j.bbrc.2013.11.042;
RA Lien H.W., Yang C.H., Cheng C.H., Liao Y.F., Han Y.S., Huang C.J.;
RT "Zinc finger protein 219-like (ZNF219L) and Sox9a regulate synuclein-gamma2
RT (sncgb) expression in the developing notochord of zebrafish.";
RL Biochem. Biophys. Res. Commun. 442:189-194(2013).
CC -!- FUNCTION: Transcriptional regulator (PubMed:24155663, PubMed:24269816).
CC Recognizes and binds to the core DNA sequence motif 5'-GGGGG-3'
CC (PubMed:24155663, PubMed:24269816). Binds to the col2a1a promoter and
CC activates col2a1a expression (PubMed:24155663). Binds to the sncgb
CC promoter and activates sncgb expression, as part of a complex with
CC sox9a (PubMed:24269816). {ECO:0000269|PubMed:24155663,
CC ECO:0000269|PubMed:24269816}.
CC -!- SUBUNIT: Interacts with sox9a. {ECO:0000269|PubMed:24269816}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:24155663,
CC ECO:0000305|PubMed:24269816}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and brain. Also detected
CC at lower levels in muscle and testis. {ECO:0000269|PubMed:24155663}.
CC -!- DEVELOPMENTAL STAGE: Detected in the notochord at 22-48 hours post-
CC fertilization (hpf). Expressed in otic vesicles and pectoral fin at 48
CC hpf. Expressed in the hindbrain and midbrain-hindbrain boundary at 48-
CC 96 hpf. {ECO:0000269|PubMed:24155663}.
CC -!- DOMAIN: C2H2-type zinc-finger domains 6 and 9 are important for binding
CC to the GGGGG motif in target DNA, and for the interaction with sox9a.
CC {ECO:0000269|PubMed:24155663, ECO:0000269|PubMed:24269816}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in a
CC curved body axis (PubMed:24155663). Expression of col2a1a and sncgb in
CC the developing notochord at 24 hours post-fertilization is
CC significantly reduced (PubMed:24155663, PubMed:24269816).
CC {ECO:0000269|PubMed:24155663, ECO:0000269|PubMed:24269816}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; JX141438; AGE89832.1; -; mRNA.
DR EMBL; AL929105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX664721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001277346.1; NM_001290417.1.
DR AlphaFoldDB; F1QQA8; -.
DR STRING; 7955.ENSDARP00000097852; -.
DR PaxDb; F1QQA8; -.
DR Ensembl; ENSDART00000110544; ENSDARP00000097852; ENSDARG00000079738.
DR GeneID; 102997060; -.
DR KEGG; dre:102997060; -.
DR CTD; 51222; -.
DR ZFIN; ZDB-GENE-110623-1; znf219.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156397; -.
DR HOGENOM; CLU_008125_1_0_1; -.
DR InParanoid; F1QQA8; -.
DR OMA; LTIWRHV; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF332241; -.
DR PRO; PR:F1QQA8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000079738; Expressed in brain and 20 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:CACAO.
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:0030903; P:notochord development; IMP:ZFIN.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1095
FT /note="Zinc finger protein 219"
FT /id="PRO_0000442538"
FT ZN_FING 153..175
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..299
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..325
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..607
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 699..721
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 727..749
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 929..952
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 591
FT /note="G -> D (in Ref. 1; AGE89832)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="G -> V (in Ref. 1; AGE89832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1095 AA; 117891 MW; 82853D8D31B59694 CRC64;
MDSPPECMLA LSCEPPLSPP SMPSLDHSPQ FLPQSPQSTP SSPQTELYAP VSPCPLPEAS
LQDEEEEDEE LSTPPSPTPA VALFPGELEL GSPSSESSPP ATPLAPFPSF GALEKAISSG
QSTTCNDELD LQLFNNESIA VTGGTSSGPG LRFPCHVCGK RFRFQSILSL HARAHSLDRE
RRASAPYRTT HSKLQQNHES NSMIQNPLSG SFQKSMNEDM VPEEPLQTAS SPQFLFEGTT
ALTPPLTEEA PISTSFSPLG HAQLEDNTPS PAAPAFRCHA CKGKFRTASE LARHVRILHN
PYKCTMCPFS ASQEERLAAH LQESHPPEDP PAEAVFPSGA IKAPPETPVP QMSVIPAFRC
ETCGQRFTQS WFLKGHMRKH KDSLDHKCQV CGRGFKEPWF LKNHMKVHLN KLGLKAGLGN
LGPPGADQSK GPASSQVLGA LYSNLLLARS MAGGGGSGSR TERSDASAGS SKSSILGYLG
LPKDSSNGSC MERLQAVAQV AEMGNGGGRG GDSADGADQA AMWQLVARSL VAAQHNQQQQ
QQQRSHSLHQ HPSSRATVAG EAKNMRAYLG GLGSREELDG SSAPWECPDC GKLFRSLQQV
VAHAHVHVQK TQKGQSARGG MSREEDIINR VSGTQATGGA GQRTGENESR QEGKQLPSGV
GASGSFHSVI SHLSGQNGLR GSSPSSSSPR ERVRGTGMKD CPYCGKAFRS SHHLKVHLRV
HTGERPYKCP HCDYAGTQSG SLKYHLQRHH REQRNAMATS PNSPSPSLPS LTGSPREGAK
KRRLPSMSQQ SSFGRVPGEA PSSRHTQSWT IGLSEKKEGS SASAHHREGD LESQYRGLSG
MMGALLPSGL EQSWIGEVTL PKVPKVSRRK PQITSRMVSA NGFQDKMTSQ EGGFEPLDLS
RRPLQDEGGV SQSGSGPSSG SKGGNDILNQ CVFCPFRTSS VELMAMHLQV NHTSKSRRKR
GAPISSNNHS QKLARPDRDP LALWKFLGVE DGVASPEDWV SARAENGVSP ENRETEDNLE
LASGAMGSFR SRKKKPQMSE HVDEEDEEID EEENDLEANG SFANVPQNQS RRAQSVSSDL
PDDDLPKEEE GVLGE
