ID   ZN423_RAT               Reviewed;        1311 AA.
AC   O08961; Q63681;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Zinc finger protein 423;
DE   AltName: Full=Olf1/EBF-associated zinc finger protein;
DE            Short=rOAZ;
DE   AltName: Full=Smad- and Olf-interacting zinc finger protein;
GN   Name=Znf423; Synonyms=Oaz, Zfp423;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aorta;
RA   Patel C.V., Gorski D.H., Walsh K.;
RT   "Zinc finger protein coding cDNA from adult rat aorta.";
RL   Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-1311, FUNCTION, DNA-BINDING, TISSUE
RP   SPECIFICITY, DOMAIN, AND INTERACTION WITH EBF1.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9151733; DOI=10.1523/jneurosci.17-11-04159.1997;
RA   Tsai R.Y.L., Reed R.R.;
RT   "Cloning and functional characterization of Roaz, a zinc finger protein
RT   that interacts with O/E-1 to regulate gene expression: implications for
RT   olfactory neuronal development.";
RL   J. Neurosci. 17:4159-4169(1997).
RN   [3]
RP   DOMAIN, DNA-BINDING, AND SUBUNIT.
RX   PubMed=9774661; DOI=10.1128/mcb.18.11.6447;
RA   Tsai R.Y.L., Reed R.R.;
RT   "Identification of DNA recognition sequences and protein interaction
RT   domains of the multiple-Zn-finger protein Roaz.";
RL   Mol. Cell. Biol. 18:6447-6456(1998).
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 via its interaction with EBF1, a
CC       transcription factor involved in terminal olfactory receptor neurons
CC       differentiation; this interaction preventing EBF1 to bind DNA and
CC       activate olfactory-specific genes. Involved in olfactory neurogenesis
CC       by participating in a developmental switch that regulates the
CC       transition from differentiation to maturation in olfactory receptor
CC       neurons. Controls proliferation and differentiation of neural
CC       precursors in cerebellar vermis formation.
CC       {ECO:0000269|PubMed:9151733}.
CC   -!- SUBUNIT: Homodimer. Interacts with PARP1, SMAD1 and SMAD4 (By
CC       similarity). Interacts with EBF1. Interacts with CEP290 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, eye, olfactory epithelium,
CC       spleen and heart. Expressed in the basal layer, consisting of neural
CC       precursor cells and immature sensory neurons of the olfactory
CC       epithelium, but not in the mature receptor cells.
CC       {ECO:0000269|PubMed:9151733}.
CC   -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC       regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type
CC       zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while
CC       zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8
CC       bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc
CC       fingers 9-13 bind BMP target gene promoters in concert with SMADs (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42353.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB58646.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L03386; AAA42353.1; ALT_FRAME; mRNA.
DR   EMBL; U92564; AAB58646.1; ALT_INIT; mRNA.
DR   PIR; T33754; T33754.
DR   PIR; T34020; T34020.
DR   RefSeq; NP_446035.2; NM_053583.2.
DR   AlphaFoldDB; O08961; -.
DR   BMRB; O08961; -.
DR   BioGRID; 250171; 1.
DR   STRING; 10116.ENSRNOP00000020028; -.
DR   PhosphoSitePlus; O08961; -.
DR   PaxDb; 10116-ENSRNOP00000020028; -.
DR   KEGG; rno:94188; -.
DR   AGR; RGD:621664; -.
DR   CTD; 94187; -.
DR   RGD; 621664; Zfp423.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; O08961; -.
DR   OrthoDB; 3073634at2759; -.
DR   PhylomeDB; O08961; -.
DR   PRO; PR:O08961; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR   GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISO:RGD.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:RGD.
DR   GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
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; 2.
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   1: Evidence at protein level;
KW   Activator; Developmental protein; Differentiation; DNA-binding;
KW   Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1311
FT                   /note="Zinc finger protein 423"
FT                   /id="PRO_0000308597"
FT   ZN_FING         75..101
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         146..168
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         174..196
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         202..224
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         230..252
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..294
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         303..326
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         331..353
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         436..460
FT                   /note="C2H2-type 9; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         468..491
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         507..530
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         544..567
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         590..615
FT                   /note="C2H2-type 13; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         659..681
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         689..711
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         719..742
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         747..770
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         777..800
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         808..830
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         834..857
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         913..935
FT                   /note="C2H2-type 21; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         957..979
FT                   /note="C2H2-type 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         986..1008
FT                   /note="C2H2-type 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1047..1069
FT                   /note="C2H2-type 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1091..1109
FT                   /note="C2H2-type 25; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1147..1170
FT                   /note="C2H2-type 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1195..1217
FT                   /note="C2H2-type 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1225..1247
FT                   /note="C2H2-type 28"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1256..1279
FT                   /note="C2H2-type 29"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1286..1309
FT                   /note="C2H2-type 30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1163..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
FT   MOD_RES         1081
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M1K9"
SQ   SEQUENCE   1311 AA;  147227 MW;  6A5680DA502B7E36 CRC64;
     MSRRKQAKPR SVKVEEGEAS DFSLAWDSSV AAAGGLEGES ECDRKSSRAL EDRNSVTSQE
     ERNEDDEDVE DESIYTCDHC QQDFESLADL TDHRAHRCPG DGDDDPQLSW VASSPSSKDV
     ASPTQMIGDG CDLGLGEEEG GTGLPYPCQF CDKSFIRLSY LKRHEQIHSD KLPFKCTFCS
     RLFKHKRSRD RHIKLHTGDK KYHCHECEAA FSRRDHLKIH LKTHSSSKPF KCSVCKRGFS
     STSSLQSHMQ AHKKNKEHLA KSEKEAKKDD FMCDYCEDTF SQTEELEKHV LTLHPQLSEK
     ADLQCIHCPE VFVDESTLLA HIHQAHANQK HKCPMCPEQF SSVEGVYCHL DSHRQPDSSN
     HSVSPDPVLG SVASMSSATP DSTPDPVLGS VASMSSATPD SSASVERGST PDSTLKPLRG
     QKKMRDDGQS WSKVVYSCPY CSKRDFTSLA VLEIHLKTIH ADKPQQSHTC QICLDSMPTL
     YNLNEHVRKL HKSHAYPVMQ FGNISAFHCN YCPEMFADIN SLQEHIRVSH CGPNANPPDG
     NNAFFCNQCS MGFLTESSLT EHIQQAHCSV GSTKLESPVI QPTQSFMEVY SCPYCTNSPI
     FGSILKLTKH IKENHKNIPL AHSKKSKAEQ SPVSSDVEVS SPKRQRLSGS ANSISNGEYP
     CNQCDLKFSN FESFQTHLKL HLELLLRKQA CPQCKEDFDS QESLLQHLTV HYMTTSTHYV
     CESCDKQFSS VDDLQKHLLD MHTFVLYHCT LCQEVFDSKV SIQVHLAVKH SNEKKMYRCT
     ACNWDFRKEA DLQVHVKHSH LGNPAKAHKC IFCGETFSTE VELQCHITTH SKKYNCRFCS
     KAFHAVLLLE KHLREKHCVF DPAAENGTAN GVPPTSTKKA EPADLQGMLL KNPEAPNSHE
     ASEDDVDASE PMYGCDICGA AYTMEVLLQN HRLRDHNIRP GEDDGSRKKA EFIKGSHKCN
     VCSRTFFSEN GLREHLQTHR GPAKHYMCPI CGERFPSLLT LTEHKVTHSK SLDTGTCRIC
     KMPLQSEEEF IEHCQMHPDL RNSLTGFRCV VCMQTVTSTL ELKIHGTFHM QKLAGSSAAS
     SPNGQGLQKL YKCALCLKEF RSKQDLVRLD VNGLPYGLCA GCMARSANGQ VGGLAPPEPA
     DRPCAGLRCP ECNVKFESAE DLESHMQVDH RDLTPETSGP RKGAQTSPVP RKKTYQCIKC
     QMTFENEREI QIHVANHMIE EGINHECKLC NQMFDSPAKL LCHLIEHSFE GMGGTFKCPV
     CFTVFVQANK LQQHIFAVHG QEDKIYDCSQ CPQKFFFQTE LQNHTMSQHA Q
//