ZN703_DANRE
ID ZN703_DANRE Reviewed; 589 AA.
AC Q90ZE2; Q90YM7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc finger protein 703;
DE AltName: Full=NocA-like zinc finger protein 1;
DE AltName: Full=NocA-related zinc finger protein 1;
GN Name=znf703; Synonyms=nlz, nlz1, noz1; ORFNames=si:dkey-158j20.1;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=11307172; DOI=10.1002/dvdy.1119;
RA Sagerstroem C.G., Kao B.A., Lane M.E., Sive H.;
RT "Isolation and characterization of posteriorly restricted genes in the
RT zebrafish gastrula.";
RL Dev. Dyn. 220:402-408(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=11404087; DOI=10.1016/s0925-4773(01)00359-8;
RA Andreazzoli M., Broccoli V., Dawid I.B.;
RT "Cloning and expression of noz1, a zebrafish zinc finger gene related to
RT Drosophila nocA.";
RL Mech. Dev. 104:117-120(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH GROUCHO, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14550789; DOI=10.1016/s0012-1606(03)00388-9;
RA Runko A.P., Sagerstroem C.G.;
RT "Nlz belongs to a family of zinc-finger-containing repressors and controls
RT segmental gene expression in the zebrafish hindbrain.";
RL Dev. Biol. 262:254-267(2003).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15042707; DOI=10.1002/dvdy.20001;
RA Hoyle J., Tang Y.P., Wiellette E.L., Wardle F.C., Sive H.;
RT "nlz gene family is required for hindbrain patterning in the zebrafish.";
RL Dev. Dyn. 229:835-846(2004).
RN [7]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH NLZ2, SUBCELLULAR LOCATION,
RP ALTERNATIVE INITIATION, AND MUTAGENESIS OF MET-61.
RX PubMed=14709556; DOI=10.1074/jbc.m310076200;
RA Runko A.P., Sagerstroem C.G.;
RT "Isolation of nlz2 and characterization of essential domains in Nlz family
RT proteins.";
RL J. Biol. Chem. 279:11917-11925(2004).
RN [8]
RP FUNCTION.
RX PubMed=19014486; DOI=10.1186/1471-213x-8-108;
RA Nakamura M., Choe S.K., Runko A.P., Gardner P.D., Sagerstroem C.G.;
RT "Nlz1/Znf703 acts as a repressor of transcription.";
RL BMC Dev. Biol. 8:108-108(2008).
CC -!- FUNCTION: Transcriptional corepressor which does not bind directly to
CC DNA and may regulate transcription through recruitment of histone
CC deacetylases to gene promoters. Required for segmental gene expression
CC during hindbrain development. May regulate cell adhesion, migration and
CC proliferation. {ECO:0000269|PubMed:14550789,
CC ECO:0000269|PubMed:14709556, ECO:0000269|PubMed:15042707,
CC ECO:0000269|PubMed:19014486}.
CC -!- SUBUNIT: Self-associates. Interacts with nlz2. May interact with
CC Groucho corepressor proteins. {ECO:0000269|PubMed:14550789,
CC ECO:0000269|PubMed:14709556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14550789,
CC ECO:0000269|PubMed:14709556}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q90ZE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q90ZE2-2; Sequence=VSP_026399;
CC -!- DEVELOPMENTAL STAGE: Expressed in a caudal domain whose anterior
CC boundary expands from the r3/r4 boundary during late gastrulation to r2
CC during somitogenesis stages. Also expressed at the midbrain to
CC hindbrain boundary by the 3-somite stage, where expression intensifies
CC by the 6 somite stage. Also expressed in the spinal cord and tailbud.
CC {ECO:0000269|PubMed:11307172, ECO:0000269|PubMed:11404087,
CC ECO:0000269|PubMed:14550789, ECO:0000269|PubMed:15042707}.
CC -!- SIMILARITY: Belongs to the Elbow/Noc 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; AF222996; AAK73547.1; -; mRNA.
DR EMBL; AY026937; AAK08969.1; -; mRNA.
DR EMBL; BX927172; CAK05188.1; -; Genomic_DNA.
DR EMBL; BC095600; AAH95600.1; -; mRNA.
DR RefSeq; NP_571897.1; NM_131822.1. [Q90ZE2-1]
DR AlphaFoldDB; Q90ZE2; -.
DR STRING; 7955.ENSDARP00000051552; -.
DR PaxDb; Q90ZE2; -.
DR Ensembl; ENSDART00000051553; ENSDARP00000051552; ENSDARG00000035563. [Q90ZE2-1]
DR Ensembl; ENSDART00000192023; ENSDARP00000149772; ENSDARG00000112912. [Q90ZE2-1]
DR GeneID; 114429; -.
DR KEGG; dre:114429; -.
DR CTD; 80139; -.
DR ZFIN; ZDB-GENE-010717-1; znf703.
DR eggNOG; ENOG502QV57; Eukaryota.
DR GeneTree; ENSGT00390000014618; -.
DR HOGENOM; CLU_035082_1_0_1; -.
DR InParanoid; Q90ZE2; -.
DR OMA; SQAPHMD; -.
DR PhylomeDB; Q90ZE2; -.
DR TreeFam; TF324968; -.
DR Reactome; R-DRE-212436; Generic Transcription Pathway.
DR PRO; PR:Q90ZE2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035563; Expressed in tail bud paraxial mesoderm and 26 other tissues.
DR ExpressionAtlas; Q90ZE2; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:ZFIN.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003677; F:DNA binding; ISS:ZFIN.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:ZFIN.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IGI:ZFIN.
DR GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:ZFIN.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:ZFIN.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR022129; Tscrpt_rep_NocA-like.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF12402; nlz1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; Developmental protein; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..589
FT /note="Zinc finger protein 703"
FT /id="PRO_0000292208"
FT ZN_FING 462..490
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 102..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..460
FT /note="Required for interaction with Groucho and hdac2
FT plays an important role in repression of transcription"
FT REGION 498..589
FT /note="Required for self-association and nuclear
FT localization"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026399"
FT MUTAGEN 61
FT /note="M->G: Abrogates initiation of translation of isoform
FT 2."
FT /evidence="ECO:0000269|PubMed:14709556"
FT CONFLICT 339
FT /note="A -> T (in Ref. 2; AAK08969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 61572 MW; 73A1268E4AC85A34 CRC64;
MSELPPGFAV SPRNQQTFKS HYITNDSSPT CLGLQVDSIA SLPYRDPARQ EKRLPIRILK
MLTAHTSHIL HPEYLQPLSS APVSIELDAK KSPLALLAQT CSQIGKPDPP PSSKLGSLSS
SSHGDKDSRS SSSSLKSGEH QNLDDKSSFK PYSKTGSECR KEGAGINSSA DKAGFRVPNG
SSSSVTCTSL PPHAPSPRAS SPQQTSGQSH THRQSQSPLS QKTAHLQTTH MDSKAAGSDP
GNDSSSSGSD RNGKKDSDHN KSSLDVVQIA NSSHARASVN SSSASSSSSP QPDSKTDSQP
PQPSLGTGHI APVSPFKPGH SVFPLPSSTM GYHGSIVGAY TGYPSQFVPG LDPAKSSLGM
GVPGKHPSSS PLTGASPPSF MQGLCRDPYC LTYPNAPHLG GSNCSSCVHD PSSALKSGFP
LMYPTHHLHS LHPSSLSSSA TSSLSHPLYT YGFMLPNETL PHACNWVSVG GPCDKRFATS
EELLAHLRTH TALPGVDGKL LSGYPSSVSS AASCHLHLPP PSSPGALPSS LSLRGSPGLG
LARYHPYGKA HLPGAPSLPM HSLPATAPYY SPYALYSQRL GSASALGYQ
