ID   AEBP2_XENLA             Reviewed;         358 AA.
AC   Q6GR30;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Zinc finger protein aebp2;
DE   AltName: Full=Adipocyte enhancer-binding protein 2 homolog;
DE            Short=AE-binding protein 2 homolog;
GN   Name=aebp2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding transcriptional repressor. May interact with and
CC       stimulate the activity of histone methyltransferase complexes.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family.
CC       {ECO:0000305}.
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DR   EMBL; BC071104; AAH71104.1; -; mRNA.
DR   RefSeq; NP_001085340.1; NM_001091871.1.
DR   AlphaFoldDB; Q6GR30; -.
DR   SMR; Q6GR30; -.
DR   DNASU; 443766; -.
DR   GeneID; 443766; -.
DR   KEGG; xla:443766; -.
DR   CTD; 443766; -.
DR   Xenbase; XB-GENE-6251879; aebp2.S.
DR   OrthoDB; 959457at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 443766; Expressed in blastula and 19 other tissues.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..358
FT                   /note="Zinc finger protein aebp2"
FT                   /id="PRO_0000341593"
FT   ZN_FING         108..133
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         147..169
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         175..199
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  38967 MW;  E3F5C915DAD7A0FF CRC64;
     MAAACECPEP SAPPAGSSAE SEVPPAGEEE DEADDESSRS SGSGRESQGP EGGGGAGSLA
     VSEAEPLSRM DSEDSISSTL MDVDSTVSSG RSTPAMMNGG SANKNLSYSC CWDHCQTPFS
     CSPDLADHIR SIHVDGQHGG VYVCYWKGCK VYNTPSTSHS WLQRHMLTHS GDKPFKCVVG
     DCNASFASQG GLARHVPTHF SQQNSSKMAN HSKSKEESPS KAGLNRKKKL KIKRKRALAR
     PYDFFDAQTL DAIRHRAICF NLCAQIESLG NGHSVVFHST VIAKRKEETG KIKLLLHWTP
     EDILPDVWVN ESDRHQQKTK VVHLSKLPKD TALLLDPNIY RNSSKRNTHI GTLKEHLS