ID   HIC2_DANRE              Reviewed;         560 AA.
AC   Q90W33;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Hypermethylated in cancer 2 protein;
GN   Name=hic2; Synonyms=hrg22;
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 {ECO:0000312|EMBL:CAC70661.1};
RN   [1] {ECO:0000312|EMBL:CAC70661.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo {ECO:0000269|PubMed:11554746};
RX   PubMed=11554746; DOI=10.1006/bbrc.2001.5624;
RA   Deltour S., Pinte S., Guerardel C., Leprince D.;
RT   "Characterization of HRG22, a human homologue of the putative tumor
RT   suppressor gene HIC1.";
RL   Biochem. Biophys. Res. Commun. 287:427-434(2001).
CC   -!- FUNCTION: Transcriptional repressor. {ECO:0000250|UniProtKB:Q96JB3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. Hic subfamily. {ECO:0000305}.
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DR   EMBL; AJ307688; CAC70661.1; -; mRNA.
DR   AlphaFoldDB; Q90W33; -.
DR   SMR; Q90W33; -.
DR   PRIDE; Q90W33; -.
DR   Ensembl; ENSDART00000160046; ENSDARP00000137761; ENSDARG00000100497.
DR   Ensembl; ENSDART00000183223; ENSDARP00000150630; ENSDARG00000100497.
DR   ZFIN; ZDB-GENE-030619-1; hic2.
DR   GeneTree; ENSGT00940000159978; -.
DR   HOGENOM; CLU_015352_2_0_1; -.
DR   InParanoid; Q90W33; -.
DR   OMA; HTPQELP; -.
DR   PhylomeDB; Q90W33; -.
DR   PRO; PR:Q90W33; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 10.
DR   Bgee; ENSDARG00000100497; Expressed in blastula and 20 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..560
FT                   /note="Hypermethylated in cancer 2 protein"
FT                   /id="PRO_0000046947"
FT   DOMAIN          24..87
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037,
FT                   ECO:0000305"
FT   ZN_FING         387..409
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000305"
FT   ZN_FING         450..472
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000305"
FT   ZN_FING         478..500
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000305"
FT   ZN_FING         506..528
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000305"
FT   ZN_FING         534..556
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000305"
FT   REGION          122..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  62600 MW;  A744CC3E5C13F3EA CRC64;
     MELPNHAKQL LLQLNQQRAK GYLCDVIIVV ENALFRAHKN ILAASSIYFK SLILHDNLIN
     LDTDMVNPSV FRQVLDFIYT GKLLSSDQFS DHNFNALLTA ASYLQLHDLA ALCRKKLKRN
     GRSLLNKPTT PTNGRTSRNQ RLSSTPVTPN QMSGLKDSEK TKRHEELIKD DLSEDEMFAR
     NTHCTTSNSL SPSTSKNGSN GSCGMQELGL DLSKKSPSGS TATEEVSPSS IPQESPQSAS
     ESTANSASFD ENPNTQNLTA GEPMELGVGE CEESQPPPDV DQHKSSRQVT RQRRQPKSEG
     KKGEDMERVT LPNGVSKRLK VAGERLPAGG NGNSEVSFQC KDEEEGLENG QEQSEESGQS
     ENEGGRNSAN YVYRQEGFEP ALGDNLYVCI PCGKGFPSSE ELNAHVETHT EEELYIKEED
     DDSYPKEDEV EAEDLSSQIT QVHGTETRRF SCSVCNKSYK DPATLRQHEK THWLTRPFPC
     NICGKMFTQR GTMTRHMRSH LGLKPFACEE CGMRFTRQYR LTEHMRVHSG EKPYECQLCG
     GKFTQQRNLI SHLRMHTSPS