ZN423_DANRE
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 03-AUG-2022, entry version 105.
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.ENSDARP00000077731; -.
DR PaxDb; A1L1R6; -.
DR PeptideAtlas; A1L1R6; -.
DR PRIDE; A1L1R6; -.
DR Ensembl; ENSDART00000189493; ENSDARP00000146416; ENSDARG00000059707.
DR GeneID; 566696; -.
DR KEGG; dre:566696; -.
DR ZFIN; ZDB-GENE-030131-4368; znf423.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158492; -.
DR HOGENOM; CLU_004018_0_0_1; -.
DR InParanoid; A1L1R6; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A1L1R6; -.
DR TreeFam; TF331504; -.
DR PRO; PR:A1L1R6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000059707; Expressed in retina and 20 other tissues.
DR ExpressionAtlas; A1L1R6; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; 30.
DR SUPFAM; SSF57667; SSF57667; 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
