Zinc finger protein 423 - Rattus norvegicus (Rat)

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O08961 (ZN423_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Zinc finger protein 423

Alternative name(s):
Olf1/EBF-associated zinc finger protein
Short name=rOAZ
Smad- and Olf-interacting zinc finger protein

Gene names

Name:	Znf423
Synonyms:	Oaz, Zfp423

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1311 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. Ref.2
Subunit structure	Homodimer. Interacts with PARP1, SMAD1 and SMAD4 By similarity. Interacts with EBF1. Interacts with CEP290 By similarity. Ref.2 Ref.3
Subcellular location	Nucleus By similarity.
Tissue specificity	Expressed in brain, eye, olfactory epithelium, spleen and heart. Expressed in the basal layer, consisting of neural precursor cells and immature sensory neurons of the olfactory epithelium, but not in the mature receptor cells. Ref.2
Domain	Uses different DNA- and protein-binding zinc fingers to regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8 bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc fingers 9-13 bind BMP target gene promoters in concert with SMADs By similarity. Ref.2 Ref.3
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 30 C2H2-type zinc fingers.
Sequence caution	The sequence AAA42353.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAB58646.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: RGD nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of BMP signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	protein homodimerization activity Inferred from direct assay Ref.3. Source: RGD sequence-specific DNA binding Inferred from direct assay Ref.3. Source: RGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1311

1311

Zinc finger protein 423

PRO_0000308597

Regions

Zinc finger

75 – 101

C2H2-type 1; degenerate

Zinc finger

146 – 168

C2H2-type 2

Zinc finger

174 – 196

C2H2-type 3

Zinc finger

202 – 224

C2H2-type 4

Zinc finger

230 – 252

C2H2-type 5

Zinc finger

271 – 294

C2H2-type 6

Zinc finger

303 – 326

C2H2-type 7

Zinc finger

331 – 353

C2H2-type 8

Zinc finger

436 – 460

C2H2-type 9; degenerate

Zinc finger

468 – 491

C2H2-type 10

Zinc finger

507 – 530

C2H2-type 11

Zinc finger

544 – 567

C2H2-type 12

Zinc finger

590 – 615

C2H2-type 13; atypical

Zinc finger

659 – 681

C2H2-type 14

Zinc finger

689 – 711

C2H2-type 15

Zinc finger

719 – 742

C2H2-type 16

Zinc finger

747 – 770

C2H2-type 17

Zinc finger

777 – 800

C2H2-type 18

Zinc finger

808 – 830

C2H2-type 19

Zinc finger

834 – 857

C2H2-type 20

Zinc finger

913 – 935

C2H2-type 21; degenerate

Zinc finger

957 – 979

C2H2-type 22

Zinc finger

986 – 1008

C2H2-type 23

Zinc finger

1047 – 1069

C2H2-type 24

Zinc finger

1091 – 1109

C2H2-type 25; degenerate

Zinc finger

1147 – 1170

C2H2-type 26

Zinc finger

1195 – 1217

C2H2-type 27

Zinc finger

1225 – 1247

C2H2-type 28

Zinc finger

1256 – 1279

C2H2-type 29

Zinc finger

1286 – 1309

C2H2-type 30

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

631

Phosphoserine By similarity

Modified residue

1081

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O08961 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 6A5680DA502B7E36
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FASTA

1,311

147,227

        10         20         30         40         50         60 
MSRRKQAKPR SVKVEEGEAS DFSLAWDSSV AAAGGLEGES ECDRKSSRAL EDRNSVTSQE 

        70         80         90        100        110        120 
ERNEDDEDVE DESIYTCDHC QQDFESLADL TDHRAHRCPG DGDDDPQLSW VASSPSSKDV 

       130        140        150        160        170        180 
ASPTQMIGDG CDLGLGEEEG GTGLPYPCQF CDKSFIRLSY LKRHEQIHSD KLPFKCTFCS 

       190        200        210        220        230        240 
RLFKHKRSRD RHIKLHTGDK KYHCHECEAA FSRRDHLKIH LKTHSSSKPF KCSVCKRGFS 

       250        260        270        280        290        300 
STSSLQSHMQ AHKKNKEHLA KSEKEAKKDD FMCDYCEDTF SQTEELEKHV LTLHPQLSEK 

       310        320        330        340        350        360 
ADLQCIHCPE VFVDESTLLA HIHQAHANQK HKCPMCPEQF SSVEGVYCHL DSHRQPDSSN 

       370        380        390        400        410        420 
HSVSPDPVLG SVASMSSATP DSTPDPVLGS VASMSSATPD SSASVERGST PDSTLKPLRG 

       430        440        450        460        470        480 
QKKMRDDGQS WSKVVYSCPY CSKRDFTSLA VLEIHLKTIH ADKPQQSHTC QICLDSMPTL 

       490        500        510        520        530        540 
YNLNEHVRKL HKSHAYPVMQ FGNISAFHCN YCPEMFADIN SLQEHIRVSH CGPNANPPDG 

       550        560        570        580        590        600 
NNAFFCNQCS MGFLTESSLT EHIQQAHCSV GSTKLESPVI QPTQSFMEVY SCPYCTNSPI 

       610        620        630        640        650        660 
FGSILKLTKH IKENHKNIPL AHSKKSKAEQ SPVSSDVEVS SPKRQRLSGS ANSISNGEYP 

       670        680        690        700        710        720 
CNQCDLKFSN FESFQTHLKL HLELLLRKQA CPQCKEDFDS QESLLQHLTV HYMTTSTHYV 

       730        740        750        760        770        780 
CESCDKQFSS VDDLQKHLLD MHTFVLYHCT LCQEVFDSKV SIQVHLAVKH SNEKKMYRCT 

       790        800        810        820        830        840 
ACNWDFRKEA DLQVHVKHSH LGNPAKAHKC IFCGETFSTE VELQCHITTH SKKYNCRFCS 

       850        860        870        880        890        900 
KAFHAVLLLE KHLREKHCVF DPAAENGTAN GVPPTSTKKA EPADLQGMLL KNPEAPNSHE 

       910        920        930        940        950        960 
ASEDDVDASE PMYGCDICGA AYTMEVLLQN HRLRDHNIRP GEDDGSRKKA EFIKGSHKCN 

       970        980        990       1000       1010       1020 
VCSRTFFSEN GLREHLQTHR GPAKHYMCPI CGERFPSLLT LTEHKVTHSK SLDTGTCRIC 

      1030       1040       1050       1060       1070       1080 
KMPLQSEEEF IEHCQMHPDL RNSLTGFRCV VCMQTVTSTL ELKIHGTFHM QKLAGSSAAS 

      1090       1100       1110       1120       1130       1140 
SPNGQGLQKL YKCALCLKEF RSKQDLVRLD VNGLPYGLCA GCMARSANGQ VGGLAPPEPA 

      1150       1160       1170       1180       1190       1200 
DRPCAGLRCP ECNVKFESAE DLESHMQVDH RDLTPETSGP RKGAQTSPVP RKKTYQCIKC 

      1210       1220       1230       1240       1250       1260 
QMTFENEREI QIHVANHMIE EGINHECKLC NQMFDSPAKL LCHLIEHSFE GMGGTFKCPV 

      1270       1280       1290       1300       1310 
CFTVFVQANK LQQHIFAVHG QEDKIYDCSQ CPQKFFFQTE LQNHTMSQHA Q

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References

[1]	"Zinc finger protein coding cDNA from adult rat aorta." Patel C.V., Gorski D.H., Walsh K. Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Aorta.
[2]	"Cloning and functional characterization of Roaz, a zinc finger protein that interacts with O/E-1 to regulate gene expression: implications for olfactory neuronal development." Tsai R.Y.L., Reed R.R. J. Neurosci. 17:4159-4169(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-1311, FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH EBF1. Strain: Sprague-Dawley.
[3]	"Identification of DNA recognition sequences and protein interaction domains of the multiple-Zn-finger protein Roaz." Tsai R.Y.L., Reed R.R. Mol. Cell. Biol. 18:6447-6456(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, DNA-BINDING, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L03386 mRNA. Translation: AAA42353.1. Frameshift. U92564 mRNA. Translation: AAB58646.1. Different initiation.
IPI	IPI00197529.
PIR	T33754. T34020.
RefSeq	NP_446035.2. NM_053583.2.
UniGene	Rn.9981.
3D structure databases
HSSP	HSSP built from PDB template 1SP1 based on UniProtKB P08047.
ProteinModelPortal	O08961.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000020028.
Proteomic databases
PaxDb	O08961.
PRIDE	O08961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	94188.
KEGG	rno:94188.
Organism-specific databases
CTD	94187.
RGD	621664. Zfp423.
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000155793.
HOVERGEN	HBG052773.
InParanoid	O08961.
OrthoDB	EOG4NP72N.
Gene expression databases
ArrayExpress	O08961.
Genevestigator	O08961.
Family and domain databases
Gene3D	3.30.160.60. 4 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00096. zf-C2H2. 2 hits. [Graphical view]
SMART	SM00355. ZnF_C2H2. 30 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 27 hits. PS50157. ZINC_FINGER_C2H2_2. 23 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	617834.

Entry information

Entry name

ZN423_RAT

Accession

Primary (citable) accession number: O08961
Secondary accession number(s): Q63681

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents