ZBT17_CHICK
ID ZBT17_CHICK Reviewed; 706 AA.
AC Q90625;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Zinc finger and BTB domain-containing protein 17;
DE AltName: Full=Zinc finger protein 151;
DE AltName: Full=Zinc finger protein Z13;
DE Flags: Fragment;
GN Name=ZBTB17; Synonyms=ZNF151;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7575457; DOI=10.1042/bj3110219;
RA Schulz T.C., Hopwood B., Rathjen P.D., Wells J.R.E.;
RT "An unusual arrangement of 13 zinc fingers in the vertebrate gene Z13.";
RL Biochem. J. 311:219-224(1995).
CC -!- FUNCTION: Transcription factor that can function as an activator or
CC repressor depending on its binding partners, and by targeting negative
CC regulators of cell cycle progression. Plays a critical role in early
CC lymphocyte development, where it is essential to prevent apoptosis in
CC lymphoid precursors, allowing them to survive in response to IL7 and
CC undergo proper lineage commitment. Has been shown to bind to the
CC promoters of adenovirus major late protein and cyclin D1 and activate
CC transcription. Required for early embryonic development during
CC gastrulation. Represses RB1 transcription.
CC {ECO:0000250|UniProtKB:Q13105}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U14555; AAA21556.1; -; mRNA.
DR AlphaFoldDB; Q90625; -.
DR SMR; Q90625; -.
DR STRING; 9031.ENSGALP00000039023; -.
DR VEuPathDB; HostDB:geneid_396541; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q90625; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q90625; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..706
FT /note="Zinc finger and BTB domain-containing protein 17"
FT /id="PRO_0000047732"
FT DOMAIN <1..12
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 205..227
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..450
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..536
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 618..640
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 32..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 706 AA; 76820 MW; 4BDAAC68808F1136 CRC64;
LKSLTVLAES PVESRELLTE LGVEKVIVEG KTAARVTQGD SDKPKQVPPN QEGKEEAPVA
TAAQPKEPAE QPDAKEGPAE GQQPGGVDNA AEASPAAVSP SRPQPAESEV GNSSPGEKGS
DAPSTEARGM ELEGKEEEGE AMVEDEEEAK IPKAAQPKSE SKENAEDNES GSTDSGQENS
GETRLLRSGT YSDRTESKAY AAVTHKCEDC GKEFTHTGNF KRHIRIHTGE KPFSCRECNK
AFSDPAACKA HEKTHSPLKP YGCEECGKSY RLISLLNLHK KRHTGEAKYR CDDCGKLFTT
SGNLKRHQLV HSGEKPYQCD YCGRSFSDPT SKMRHLETHD TDKEHKCPHC DKKFNQVGNL
KAHLKIHIAD GPLKCRECGN EFTTSGNLKR HLRIHSGEKP YVCVHCQRQF ADPGALQAHV
PIHTGEKPCQ CLICGKAFTQ ASSLIAHVRH DTGEKPYVCE RCGKRFVQSS QLANHIRHHD
NIRPHKCTVC NKAFVNVGDL SKHIIIHTGE KPFLCDKCGR GFNRVDNLRS HVKTVHQGKA
GMKILEPEDG SELNIVTVAS DDMVTLATEA LAATAVTQLT VVPVAAAVTA DETEALKAEI
TKAVKQVQEA DPNTQILYAC DSCGEKFLDA TSLAQHVRIH TAQALVMFQA DTDFYQQYGA
AAATWQTEQV IPATELLFRP RDSPQEAPAA PLAPVPLAGE GQAPAE
