ZB16A_DANRE
ID ZB16A_DANRE Reviewed; 671 AA.
AC Q802Y8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Zinc finger and BTB domain-containing protein 16-A {ECO:0000312|EMBL:AAH46887.1};
DE AltName: Full=Promyelocytic leukemia zinc finger protein-A;
DE AltName: Full=Zinc finger protein PLZF-A {ECO:0000303|PubMed:20080956};
GN Name=zbtb16a {ECO:0000312|ZFIN:ZDB-GENE-030131-1989};
GN Synonyms=plzfa {ECO:0000303|PubMed:20080956},
GN zbtb16 {ECO:0000312|ZFIN:ZDB-GENE-030131-1989}; ORFNames=zgc:55675;
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;
RN [1] {ECO:0000312|EMBL:AAH46887.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH46887.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18307296};
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BTBD6A, SUBCELLULAR LOCATION, UBIQUITINATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=20080956; DOI=10.1101/gad.554510;
RA Sobieszczuk D.F., Poliakov A., Xu Q., Wilkinson D.G.;
RT "A feedback loop mediated by degradation of an inhibitor is required to
RT initiate neuronal differentiation.";
RL Genes Dev. 24:206-218(2010).
CC -!- FUNCTION: Probable transcription factor. Probable substrate-recognition
CC component of an E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). Inhibits neurogenesis.
CC {ECO:0000250|UniProtKB:Q05516, ECO:0000269|PubMed:20080956}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q05516}.
CC -!- SUBUNIT: Interacts with btbd6a (via BTB domain).
CC {ECO:0000269|PubMed:20080956}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20080956}. Cytoplasm
CC {ECO:0000269|PubMed:20080956}. Note=Nuclear export to the cytoplasm is
CC promoted by btbd6a. {ECO:0000269|PubMed:20080956}.
CC -!- TISSUE SPECIFICITY: During early stages of primary neurogenesis,
CC expressed in the neural epithelium, with highest levels in the
CC forebrain and midbrain. Also expressed in a posterior-to-anterior
CC gradient in the caudal neural plate at the 3-6 somite stage.
CC {ECO:0000269|PubMed:20080956}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000269|PubMed:20080956}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000255}.
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DR EMBL; BC046887; AAH46887.1; -; mRNA.
DR RefSeq; NP_955929.1; NM_199635.1.
DR AlphaFoldDB; Q802Y8; -.
DR SMR; Q802Y8; -.
DR BioGRID; 81611; 1.
DR STRING; 7955.ENSDARP00000115504; -.
DR iPTMnet; Q802Y8; -.
DR PaxDb; Q802Y8; -.
DR GeneID; 323269; -.
DR KEGG; dre:323269; -.
DR CTD; 323269; -.
DR ZFIN; ZDB-GENE-030131-1989; zbtb16a.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q802Y8; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q802Y8; -.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q802Y8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0032481; P:positive regulation of type I interferon production; IDA:ZFIN.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0050767; P:regulation of neurogenesis; IGI:ZFIN.
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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..671
FT /note="Zinc finger and BTB domain-containing protein 16-A"
FT /id="PRO_0000401140"
FT DOMAIN 34..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 401..423
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
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..537
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 600..622
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 628..650
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 130..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 671 AA; 74854 MW; 38F9098ED793892F CRC64;
MDLTKMGMIQ LQNPNHPNAL LHKANQMRLA GTLCDVVIMV DSQEFHAHRT VLACTSKMFE
ILFHRNSQHY TLDFLSPKTF QQILEYAYTA TLQAKVEDLD DLLYAAEILE IEYLEEQCLK
ILETIQSSDE NDTEVNMNDG GTEDDEERKG RHGRNLVGSK KHSTEESGYV SAAQQALALP
GMVDQSPSVS TSFGLSTMSP TKAAVDSLMS IGQSLLQSTM HPGVGAEQPL HGNSHPMMGE
IKTEMMQVDE SGEHESPKAM ESIASSNGER SGEPDKNRDG PGTPTRSSVI TSARELHYVR
DEGLGDQQAE VSQMGLEAMA GMTEKHLASL YGIPSNHKNE AMLSMPASMA SSLHMSPALA
MSMDFSAYGG LLPQSFIQRE FFSKLGELAA GIKPDGRSLN ERCNVCGAEL PDNEAIEQHR
KLHSGMKTYG CELCGKRFLD SLRLRMHLLS HSAGEKAIVC DQCGAQFQKE DALEAHRQIH
TGSDMAIFCL LCGKRFQTQT ALQQHMEVHA GVRSYICSEC NRTFPSHTAL KRHLRSHTAG
DHPFECEFCG SCFRDESTLK GHKRIHTGEK PYECNGCGKK FSLKHQLETH YRVHTGEKPF
ECKLCHQRSR DYSAMIKHLR THNGASPYQC TICLEYCPSL SAMQKHMKGH KPEDIPPDWR
IEKTYLYLCY V
