ID ZBT38_RAT Reviewed; 1203 AA.
AC Q5EXX3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Zinc finger and BTB domain-containing protein 38;
DE AltName: Full=Zinc finger protein expressed in neurons;
DE Short=Zenon;
GN Name=Zbtb38 {ECO:0000250|UniProtKB:Q8BW71};
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] {ECO:0000305, ECO:0000312|EMBL:AAT72920.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAT72920.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAT72920.1};
RX PubMed=15713629; DOI=10.1128/mcb.25.5.1713-1729.2005;
RA Kiefer H., Chatail-Hermitte F., Ravassard P., Bayard E., Brunet I.,
RA Mallet J.;
RT "ZENON, a novel POZ Kruppel-like DNA binding protein associated with
RT differentiation and/or survival of late postmitotic neurons.";
RL Mol. Cell. Biol. 25:1713-1729(2005).
CC -!- FUNCTION: Transcriptional regulator with bimodal DNA-binding
CC specificity. Binds with a higher affinity to methylated CpG
CC dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to
CC E-box elements (5'-CACGTG-3'). Can also bind specifically to a single
CC methyl-CpG pair. Represses transcription in a methyl-CpG-dependent
CC manner. Plays an important role in regulating DNA-replication and
CC common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent
CC manner; represses expression of MCM10 which plays an important role in
CC DNA-replication (By similarity). Acts as a transcriptional activator.
CC May be involved in the differentiation and/or survival of late
CC postmitotic neurons (PubMed:15713629). {ECO:0000250|UniProtKB:Q8NAP3,
CC ECO:0000269|PubMed:15713629, ECO:0000303|PubMed:15713629}.
CC -!- SUBUNIT: Interacts with CBFA2T3, ZBTB4 and RBBP6.
CC {ECO:0000250|UniProtKB:Q8NAP3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15713629}. Chromosome
CC {ECO:0000250|UniProtKB:Q8NAP3}. Note=Localizes to chromocenters.
CC {ECO:0000250|UniProtKB:Q8NAP3}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout the adult brain where
CC it is found mainly in neurons. Also expressed in the adrenal medulla.
CC Not detected in non-neural tissues including heart, spleen, liver and
CC muscle. In the embryo, expressed in the developing brain and spinal
CC cord but not in the migratory neural crest. Also expressed in the
CC limbs, transiently in somites, and in the embryonic liver. In the
CC embryonic neural tube, expression is restricted to late postmitotic
CC neurons. {ECO:0000269|PubMed:15713629}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult. Embryonic
CC expression is detected from 12 dpc. {ECO:0000269|PubMed:15713629}.
CC -!- DOMAIN: The BTB domain is not required for activation of transcription
CC or self-association. {ECO:0000269|PubMed:15713629}.
CC -!- PTM: Ubiquitinated by RBBP6; leading to its degradation by the
CC proteasome. {ECO:0000250|UniProtKB:Q8NAP3}.
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DR EMBL; AY623002; AAT72920.1; -; mRNA.
DR RefSeq; NP_001012489.1; NM_001012471.1.
DR AlphaFoldDB; Q5EXX3; -.
DR SMR; Q5EXX3; -.
DR BioGRID; 261189; 1.
DR STRING; 10116.ENSRNOP00000067350; -.
DR PhosphoSitePlus; Q5EXX3; -.
DR PaxDb; 10116-ENSRNOP00000067350; -.
DR GeneID; 315936; -.
DR KEGG; rno:315936; -.
DR UCSC; RGD:1310136; rat.
DR AGR; RGD:1310136; -.
DR CTD; 253461; -.
DR RGD; 1310136; Zbtb38.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5EXX3; -.
DR OrthoDB; 783166at2759; -.
DR PhylomeDB; Q5EXX3; -.
DR PRO; PR:Q5EXX3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:0008327; F:methyl-CpG binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd18223; BTB_POZ_ZBTB38_CIBZ; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
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 PANTHER; PTHR24394:SF35; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 11; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF13912; zf-C2H2_6; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 2: Evidence at transcript level;
KW Activator; Chromosome; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1203
FT /note="Zinc finger and BTB domain-containing protein 38"
FT /id="PRO_0000047743"
FT DOMAIN 33..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 341..363
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..394
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..538
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1017..1039
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1045..1067
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1073..1095
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1101..1123
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1132..1154
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 230..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..522
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT REGION 581..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 755
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 796
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 806
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 813
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 834
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 842
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 849
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 915
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 976
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 984
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 998
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1024
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1033
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT CROSSLNK 1190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NAP3"
SQ SEQUENCE 1203 AA; 135300 MW; E5E15AF3A487A12B CRC64;
MTVMSLSRDL KDDFHSDTVL SILNEQRIRG ILCDVTIIVE DTKFKAHSNV LAASSLYFKN
IFWSHTICIS SHVLELDDLK AEVFTEILNY IYSSTVVVRR QETVTDLAAA GKRLGISFLE
DLSDRNFSNS PGPYVVCITE KGVVKEEKNE KRHEEPAVTN GPRITNAFSI IETENSNSMF
SPLDLRASFK KVSDAMRTTS LCQERASVCP EAEPVRTLAE HSYAVSSITE AYRSQPLREH
DSSSSSGKTG KENGEALTTK AKPCRKPKTQ TQDSDSTTEN MPLPLVTCPE VNQERSPQPA
PILSHSEPPS SEGDVHFPRE DENQPSETPG PPAAEVPPLV YNCSCCSKSF DSSTLLGAHM
QLHKPTQDPF VCKYCNKQFT TLNRLDRHEQ ICMRSSHMPM PGGNQPFLEN YPTIGQDGGS
FTSPDSLVPE SRIGELSSAG SALSDADHMV KFVNGQMLYS CVVCKRSYVT LSSLRRHANV
HSWRRTYPCH YCNKVFALAE YRTRHEIWHT GERRYQCIFC LETFMTYYIL KNHQKSFHAI
DHRLSISKKT ANGGLKPTVY PYKLYRLLPM RCKRAPYKSY RNSSYESAQG NRQRNESPPD
TFVIPNLPSS EMPTLNFQDG RNSLTSSPAI PVETPSWQGT PTSAKVKNAE GLKWRKQALK
TDLVDSAEVS ISSIGNSVST TLQAEPVCVS SGEHSASVIS YSGLVPSVIV HSSQFSSVIK
HSNAIACLAN SNHQSPSQPV ASPSLIKDSK PEADKASKLA SRPKNSKEKK KTVPCNRGEI
TEEAKYVADL GGSSGKTTNV VEETSKIETY IAKPALPGTS TNSNVAPLCQ ITVKIGNEAI
VKRHILGSKL FYKRGRKPKY QMQEETLPRE SDPETRGDSP LGLCQADCVE MSEAFDEVSD
QDSTDKPWRP YYNYKPKKKS KQLRKIRKVK WRKERGSRSP VGRRRYPAEL DRAEMGRRRY
PAELDRCAEV KLPPDKASEE EENKEMPKLQ CELCDGDKAA GAGAEGKPHQ HLTLKPYICE
LCAKQFQSSS TLKMHMRCHT GEKPYQCKTC GRRFSVQGNL QKHERIHLGV KEFICQYCNK
AFTLNETLKI HERIHTGEKR YHCQFCFQGF LYLSTKRNHE RRHVREHDGK GFACFQCPKI
CKTAAALRMH QKKHLFKTLT KQEETDDLCH ENSDLLESQP CTDSEDSDQK DDIKKPLLKM
SFE
//
