ID ZN423_DANRE Reviewed; 1365 AA. AC A1L1R6; Q1L943; Q1LX66; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Zinc finger protein 423; GN Name=znf423; ORFNames=si:ch211-216l23.1, zgc:158272; 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; RN [1] 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Transcription factor that can both act as an activator or a CC repressor depending on the context. Plays a central role in BMP CC signaling and olfactory neurogenesis. Associates with SMADs in response CC to bmp2 leading to activate transcription of BMP target genes. Acts as CC a transcriptional repressor involved in terminal olfactory receptor CC neurons differentiation. Involved in olfactory neurogenesis by CC participating in a developmental switch that regulates the transition CC from differentiation to maturation in olfactory receptor neurons (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {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; BX470162; CAK04518.1; -; Genomic_DNA. DR EMBL; CR387935; CAK04486.1; -; Genomic_DNA. DR EMBL; BC129184; AAI29185.1; -; mRNA. DR RefSeq; NP_001073499.1; NM_001080030.1. DR AlphaFoldDB; A1L1R6; -. DR STRING; 7955.ENSDARP00000156375; -. DR PaxDb; 7955-ENSDARP00000077731; -. DR PeptideAtlas; A1L1R6; -. DR GeneID; 566696; -. DR KEGG; dre:566696; -. DR AGR; ZFIN:ZDB-GENE-030131-4368; -. DR CTD; 23090; -. DR ZFIN; ZDB-GENE-030131-4368; znf423. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_004018_0_0_1; -. DR InParanoid; A1L1R6; -. DR OrthoDB; 3073634at2759; -. DR PhylomeDB; A1L1R6; -. DR TreeFam; TF331504; -. DR PRO; PR:A1L1R6; -. DR Proteomes; UP000000437; Alternate scaffold 18. DR Proteomes; UP000000437; Chromosome 18. DR Bgee; ENSDARG00000059707; Expressed in retina and 20 other cell types or tissues. DR ExpressionAtlas; A1L1R6; baseline and differential. DR GO; GO:0005694; C:chromosome; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 14. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24406:SF8; C2H2-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR24406; TRANSCRIPTIONAL REPRESSOR CTCFL-RELATED; 1. DR Pfam; PF00096; zf-C2H2; 6. DR Pfam; PF13912; zf-C2H2_6; 3. DR SMART; SM00355; ZnF_C2H2; 30. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 23. PE 2: Evidence at transcript level; KW Activator; Developmental protein; Differentiation; DNA-binding; KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..1365 FT /note="Zinc finger protein 423" FT /id="PRO_0000308598" FT ZN_FING 76..98 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 150..172 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 178..200 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 206..228 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 234..256 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 286..309 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 318..341 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 346..368 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 437..461 FT /note="C2H2-type 9; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 469..492 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 513..536 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 555..578 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 603..628 FT /note="C2H2-type 13; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 675..697 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 705..728 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 736..759 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 764..787 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 794..817 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 831..853 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 857..880 FT /note="C2H2-type 20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 954..976 FT /note="C2H2-type 21; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1000..1022 FT /note="C2H2-type 22" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1029..1051 FT /note="C2H2-type 23" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1090..1112 FT /note="C2H2-type 24" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1201..1224 FT /note="C2H2-type 25" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1249..1271 FT /note="C2H2-type 26" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1279..1301 FT /note="C2H2-type 27" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1310..1333 FT /note="C2H2-type 28" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1340..1363 FT /note="C2H2-type 29" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 99..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 250..280 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 366..429 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 885..916 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..65 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..278 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..417 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 888..916 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1365 AA; 151465 MW; 5B53BE488AE40D49 CRC64; MSRRKQAKPR SVKAVEEAES TECASGWDSS VQTDAAVSER DSDRKESRAV GEDGEQSVTS HDERVGEEDL DDDSIFTCDN CQQDFECLAD LTEHRTNHCP ADGDDDPGLS WVASSPSSKD VASPSQMLGD GCCDMGMGTG EEEGGSGLPY PCQFCDKSFS RLSYLKRHEQ IHSDKLPFKC TFCSRLFKHK RSRDRHVKLH TGDKKYSCQE CEAAFSRSDH LKIHLKTHSS SKPFKCSICK RGFSSTSSLQ SHMQAHRKNK EHLAKKDQGK RDGSSSDVTE QDQDLYMCDY CEETFSQTDE LEKHVLTQHP QLSDRAELQC IHCPEIFSDE GTLLTHIDRT HANKKHKCPM CAEQFPSVED VYCHLDSHRQ PDSSNHSASP DPVLGSVASM SSATPDSSAS LERGSTPDST LKPGQSRRKL APSSDHDDGT WSGKVTYSCP YCSKRDFNSL AVLEIHLKTI HADKPQQSHT CQLCLETLPT LYNLNEHVRK AHRSSGNSAS NFPLLQFSNV SAFHCNYCPD MFADINSLQE HIRVSHCLSG GVVAGSTTLE GNHAFFCNQC SMGFLTESSL TEHIQQTHCS SVGGVTKMES PVLQPSQSFM EVYSCPYCTN SPIFGSLLKL TKHIKENHKN IPLANNKRKV KVADLSPASS DVEISSPKRH RVTGDSTPAV ANGDYPCNQC DLRFSSFEGF QAHLKSHLEL LLRRQSCPQC NKEDFDSQEA LLQHLTIHYT TTSTQYVCES CDKQFSSVDD LQKHLLDMHT FVLYHCTLCQ EVFDSKVSIQ VHLAVKHSNE KKMYRCTACA WDFRKESDLQ LHVKHSHLGH PASTGAPGKA RKCIFCGETF GTEVELQCHI TTHSKKYNCR LCGKAFHAIV LLERHLREKH CIFDGGNGNG NGGSQNGTPN GVTQSSKRST AGSTAAAEQA DLQNMLLKGG SQETANSHEA SGGEEELDAS EPMYACDICG AAYTMESLLQ NHRLRDHNIR PGEDDAGSRK KKADFIKGNH KCNVCSRTFF SENGLREHAQ THRGPAKHYM CPICGERFPS LLTLTEHKVT HSKSLDTGTC RICKMPLQSE EEFIEHCQMH PDLRNSLTGF RCVVCMQTVT STLELKIHGT FHMQKLSSSG GSGGGGGSAS SSPNGQLQAH KLYKCALCLK DFKNKQELVK IDVNGLPYGL CAGCMSRGTN GQSPTVVVTP QEAGDKGTTG LRCSECAVKF ETLEDLESHI QVDHTEMSPE TSGAKKVTDA SPVPKKKTYQ CIKCQMTFET EREIQIHVAN HMIEEGINHE CKLCNQMFDS PAKLLCHLIE HSFEGMGGTF KCPVCFTVFV QANKLQQHIF AVHGQEDKIY DCSQCPQKFF FQTELQNHTL SQHAQ //