ZN423_RAT
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 25-MAY-2022, entry version 139.
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};
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; 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 PaxDb; O08961; -.
DR PRIDE; O08961; -.
DR GeneID; 94188; -.
DR KEGG; rno:94188; -.
DR CTD; 94187; -.
DR RGD; 621664; Zfp423.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; O08961; -.
DR OrthoDB; 1318335at2759; -.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 transcription, DNA-templated; 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 transcription, DNA-templated; 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:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; ISO:RGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
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 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
