ID   ZN503_DANRE             Reviewed;         563 AA.
AC   Q6UFS5; Q803U2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Zinc finger protein 503;
DE   AltName: Full=NocA-like zinc finger protein 2;
GN   Name=znf503; Synonyms=nlz2;
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], FUNCTION, INTERACTION WITH NLZ1, SUBCELLULAR
RP   LOCATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- FUNCTION: Required for segmental gene expression during hindbrain
CC       development. May function as a transcriptional repressor.
CC       {ECO:0000269|PubMed:14709556, ECO:0000269|PubMed:15042707}.
CC   -!- SUBUNIT: Interacts with nlz1. {ECO:0000269|PubMed:14709556}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14709556}.
CC   -!- DEVELOPMENTAL STAGE: Detected in blastomere, near the blastoderm margin
CC       in gastrula, and in forebrain, posterior hindbrain and throughout the
CC       length of the trunk at early segmentation stages.
CC       {ECO:0000269|PubMed:14709556, 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; AY371081; AAQ72694.1; -; mRNA.
DR   EMBL; BC044193; AAH44193.1; -; mRNA.
DR   RefSeq; NP_942137.1; NM_198840.3.
DR   AlphaFoldDB; Q6UFS5; -.
DR   STRING; 7955.ENSDARP00000019426; -.
DR   PaxDb; Q6UFS5; -.
DR   Ensembl; ENSDART00000008906; ENSDARP00000019426; ENSDARG00000018492.
DR   GeneID; 324913; -.
DR   KEGG; dre:324913; -.
DR   CTD; 84858; -.
DR   ZFIN; ZDB-GENE-031113-5; znf503.
DR   eggNOG; ENOG502QUYV; Eukaryota.
DR   GeneTree; ENSGT00390000014618; -.
DR   HOGENOM; CLU_035082_1_0_1; -.
DR   InParanoid; Q6UFS5; -.
DR   OMA; SDICVAW; -.
DR   OrthoDB; 1163882at2759; -.
DR   PhylomeDB; Q6UFS5; -.
DR   TreeFam; TF324968; -.
DR   PRO; PR:Q6UFS5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000018492; Expressed in muscle tissue and 54 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:ZFIN.
DR   GO; GO:0030902; P:hindbrain development; IGI:ZFIN.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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   Developmental protein; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..563
FT                   /note="Zinc finger protein 503"
FT                   /id="PRO_0000292206"
FT   ZN_FING         431..459
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        131
FT                   /note="P -> L (in Ref. 2; AAH44193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="N -> D (in Ref. 2; AAH44193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   563 AA;  57925 MW;  DBC1D70EDF3508F7 CRC64;
     MITSPSASRN SDTDLVWESS SSSSRNNSSA VASKPFLHSV PPSDPLRQAN RLPIKILKML
     TARTGHILHP EYLQPLPSTP VSPIELDAKK SPLALLAQTC SQIGKPDPPP SSKLSSVTSN
     GSSEKESKSG PLKLSDIGVE DKSSFKPYSK PADKKDSSSG VSSGEKSGFR VPSATCQPFT
     PRTGSPNSST SASPMPSDGK GERDEKKDSD CNKNCSSDGS APTSVSHSRI SVSCAGINVE
     VNQHQETTSG SKASATSDSV SCVTSSSSAS VLGSGLVAPV SPYKPGQTVF PLPPAGMTYP
     GSLAGAYAGY PQHFLPHGGS LVNAQLASSL GCSKAGSSPL AGASPPSIMS ASLCRDPYCL
     SYHCASHLAG AAGASCTHDS AAAAAASALK SGYPLMYPTH PLHGVHSSPP SFGGHPLYPY
     GFMLPNDPLP HVCNWVSANG PCDKRFSSSE ELLNHLRTHT AFTGTEKLIS GYPSSSSLAS
     AAAAAMACHM HMPPSGAPGS PGTLALRSPH HALGLSSRYH PYSKSPLPTP GAPVPVPAAT
     GPYYSPYALY GQRLTTASAL GYQ