ID   ZN131_PONAB             Reviewed;         589 AA.
AC   Q5RAU9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Zinc finger protein 131;
GN   Name=ZNF131;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation as a repressor
CC       of ESR1/ER-alpha signaling. Plays a role during development and
CC       organogenesis as well as in the function of the adult central nervous
CC       system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Monosumoylated at Lys-567 by CBX4 and UHRF2. Sumoylation may
CC       potentiate ZNF131 inhibition of estrogen signaling. Sumoylation does
CC       not interfere with ubiquitination (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; CR858913; CAH91111.1; -; mRNA.
DR   RefSeq; NP_001127377.1; NM_001133905.1.
DR   AlphaFoldDB; Q5RAU9; -.
DR   SMR; Q5RAU9; -.
DR   STRING; 9601.ENSPPYP00000017249; -.
DR   GeneID; 100174442; -.
DR   KEGG; pon:100174442; -.
DR   CTD; 7690; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5RAU9; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR027758; Zfp131.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24403:SF55; PTHR24403:SF55; 1.
DR   Pfam; PF00651; BTB; 1.
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; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..589
FT                   /note="Zinc finger protein 131"
FT                   /id="PRO_0000047415"
FT   DOMAIN          34..98
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         254..277
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         294..316
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         322..347
FT                   /note="C2H2-type 3; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..380
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..409
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          224..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           137..148
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           283..294
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        539..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        255
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52739"
FT   CROSSLNK        261
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52739"
FT   CROSSLNK        567
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   589 AA;  67220 MW;  97F39A9F56D42BDA CRC64;
     MEAEETMECL QEFPEHHKMI LDRLNEQREQ DRFTDITLIV DGHHFKAHKA VLAACSKFFY
     KFFQEFTQEP LVEIEGVSKM AFRHLIEFTY TAKLMIQGEE EANDVWKAAE FLQMLEAIKA
     LEVRNKENSA PLEENTTGKN EAKKRKIAET SNVITESLPS AESEPVEIEV EIAEGTIEVE
     DEGVETLEEV ASAKQSVKYI QSTGSSDDSA LALLADITSK YRQGDRKGQI KEDGCPSDPT
     SKQEHMKSHS TESFKCEICN KRYLRESAWK QHLNCYHLEE GGVSKKQRTG KKIHVCQYCE
     KQFDHFGHFK EHLRKHTGEK PFECPNCHER FARNSTLKCH LTACQTGVGA KKGRKKLYEC
     QVCNSVFNSW DQFKDHLVIH TGDKPNHCTL CDLWFMQGNE LRRHLSDAHN ISERLVTEEV
     LSVETRVQTE PVTSMTIIEQ VGKVHVLPLL QVQVDSAQVT VEQVHPDLLQ GSQVHDSHMS
     ELPEQVQVSY LEVGRIQTEE GTEVHVEELH VERVNQMPVE VQTELLEADL DHATPEIMNQ
     EERESSQADA AEAAREDHED AEDLETKPTV DSEAEKAENE DRTAMPVLE