ZBT10_RAT
ID ZBT10_RAT Reviewed; 836 AA.
AC Q9WTY8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Zinc finger and BTB domain-containing protein 10;
DE AltName: Full=Zinc finger protein RIN ZF;
GN Name=Zbtb10; Synonyms=Rinzf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Insulinoma;
RX PubMed=10075714; DOI=10.1074/jbc.274.12.8123;
RA Tillotson L.G.;
RT "RIN ZF, a novel zinc finger gene, encodes proteins that bind to the CACC
RT element of the gastrin promoter.";
RL J. Biol. Chem. 274:8123-8128(1999).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
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DR EMBL; AF091457; AAD22522.1; -; mRNA.
DR RefSeq; NP_077815.1; NM_024489.1.
DR AlphaFoldDB; Q9WTY8; -.
DR SMR; Q9WTY8; -.
DR STRING; 10116.ENSRNOP00000015171; -.
DR PaxDb; Q9WTY8; -.
DR GeneID; 80338; -.
DR KEGG; rno:80338; -.
DR UCSC; RGD:708377; rat.
DR CTD; 65986; -.
DR RGD; 708377; Zbtb10.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9WTY8; -.
DR OrthoDB; 755439at2759; -.
DR PhylomeDB; Q9WTY8; -.
DR PRO; PR:Q9WTY8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..836
FT /note="Zinc finger and BTB domain-containing protein 10"
FT /id="PRO_0000047726"
FT DOMAIN 330..399
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 689..711
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 717..739
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..817
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 463
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
FT CROSSLNK 663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96DT7"
SQ SEQUENCE 836 AA; 91698 MW; E4F48AB2720676C1 CRC64;
MGPGRRGNGI GGPGAPRLGG LRRGGRRGGR QGVAAPLGHG RPRLAGRRRG GPPASGKEPS
DSGLPRGRRR GSRQQWQQSR PPGDLGVAPQ AFQWARAGGR GSGAGRAGGE GVDAGRGVPE
LQHRGGGGEP GRWQWGGRRQ RSSSRRSGGE GGEEAEGSGV GAGEGETVQH FPLARPKSLM
QKLQCSFQTS WLKDFPWLRY SNDTGLMFCG WCQTTPEDVG SVDLPQVGHD ELSRGTRNYK
KTLLLRHHVS TEHKLHEANA QVLGSQACVT VDGSAVDKPD ASEGCLLVGN ESEIPSEEGY
CDFNSRPNEN SYCYQLLRQL DEQRKKDILC DVSIVVSGKI FKAHKNILVA GSRFFKTLYC
VSNKESPNQN NTTHLDIAAV QGFSVILDFL YSGNLVLTSQ NAIEVMTVAS YLQMSEVVQT
CRNFIKDALN ISIKSEAPES VVVDYNNRKP VSRDGLTSSR DQKIASFWAT RNLTNLASNI
KIENDGCNVD EGQIENYQMN DSNWVQDGSP ELAENESQGK TKVFIWNNMA SQETGKARRK
NQTTKRFVYN IPPNSETIVE DCSVLQPPVA YPEENKALLI KEEPVSDLDG ALLSGPDGDR
TMNTNLLAEA CSSQDAGDAA GASHDFKYGL MPGTSSDFKY GLLPSTSNDF KYGLLPGAPN
DFKYGLLPES WPTQEPWENG DSSLIMNKLK CPHCSYVAKY RRTLKRHLLI HSGVRSFKCE
ICGKMFTRRE HVKRHSLVHK KDKKYKCMVC KKIFMLAASV GIKHGSRRYG VCMDCVDKSQ
PGGQESIDQG QDTEFPRDEE YEENEGVEPD EELAEDGQDQ SDAPRWDEPG GAYVSG
