ID M7AST7_CHEMY Unreviewed; 814 AA.
AC M7AST7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Zinc finger and BTB domain-containing protein 8A {ECO:0000313|EMBL:EMP28426.1};
GN ORFNames=UY3_14457 {ECO:0000313|EMBL:EMP28426.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28426.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC {ECO:0000256|ARBA:ARBA00003767}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB563787; EMP28426.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AST7; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18329; BTB_POZ_ZBTB8A_BOZF1; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
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; PTHR46105; AGAP004733-PA; 1.
DR PANTHER; PTHR46105:SF12; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 8A; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 24..92
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 321..348
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 349..377
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 657..684
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 685..713
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 191..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 92861 MW; F056DA82C50E625F CRC64;
MEISSHQFHL LQQLNEQRKQ DLFCDCCILV EGKVFKAHRN VLFASSGYFK MLLSQGSKET
SQPTTATFQA FSPDTFTVIL DFVYSGKLSL TGQNVIEVMS AASYLQMTDV ISVCKTFIKS
SLDISEKEKD RYFSLSDKDV NSNGVERSCL YGADWRTENS PPHSHLNPDQ GTCVMSGNAW
SNFSYYPASQ RNSQQQLAKH DQRQDSIKKT RHLGLQQSSD IPHYKSSKLE DRSSDPTSHI
SQSEEEVQID TEIDSAHAGY QYGQGSDVMP RSLAVSQQEH ESPHSSSKSK SSKADEQYGN
MPSILGVMGS WAEDDLPRMR FKCPFCTHVV KRKADLKRHL RCHTGERPYP CEACGKRFSR
LDHLSSHFRT IHQACKPICR KCKRHVTELT GQVVQEGTRR YRLCNECLAE AGIDSIRIDL
EAEPQLEFPQ EGDKDSRWHY SEDNRSDVEI VEDGSTDLVI QQVDDSEDEA EEQEVKPNIR
ARRKVKSNPI RSHLIPDQKA GMVNENSWTS NSNHSSSQMN VQQQETQLSK RGQKLGSVKK
RQRRLGLSQP HDFLKYKSNK PEEASGSCSA SETNCTSQSK EQIQFDAEND TAHTGYRCDQ
ESKVIPKKWS VAQLEQELSR TSPVYMDLKA DELYTSMPTI LGVMGGWNED DLPKMQFKCP
FCTHTVKRRA DMKRHLRCHT GERPYPCEAC GKKFTRLEHL RSHFQTIHQA GKLICRKCKN
HVTDLTGHVI QQGTRRYRLC NECLAEADID SIRDDLNAEH PLTISLGDKI SEWHLDEEPR
SDVEMEDEPD KFVIHQVNDD NTDETDEKVK SNLR
//
