MYNN_XENLA
ID MYNN_XENLA Reviewed; 609 AA.
AC Q6DDV0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Myoneurin;
GN Name=mynn;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC077406; AAH77406.1; -; mRNA.
DR AlphaFoldDB; Q6DDV0; -.
DR SMR; Q6DDV0; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 7.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
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 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..609
FT /note="Myoneurin"
FT /id="PRO_0000248221"
FT DOMAIN 24..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 301..323
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 329..351
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..380
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..521
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 528..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..188
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 257..262
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 68695 MW; 291D15F4697AFE95 CRC64;
MALSDHSRQL LDTLNKQRQS GFLCDCTILI GDFHFKAHRN VLASFSDYFR AYFKDSLDSI
VLLDQIKVTP SGFQTLLDFI YSGNLNYDSC NLEEINLAAQ HLRLEDVVAT CRTKIESLVG
LTKPSVTHLA PTSSSLDENE YFTSLYPREA MKVDAIEISY SQSKVKKGIK GKKSQKIKRW
KRPLRSHQHV KKKSSKCQLS SPKTPAVLSL DAKELELMAA DHVAKDNTCL LSFTSEIDCE
IFLSQNISLE TATMTQQKPA KLQQDCAMKE HCISNIADIT NVCTMEGCDK ELDPKYSKNK
PVCNTCGKVF SEASSLRRHM RIHKGVKPYV CHLCAKAFTQ CNQLKTHVRT HTGEKPYQCK
KCDKGFAQKC QLVFHSRMHH GEEKPYKCDV CNLQFATSSN LKIHARKHSG EKPYVCDRCG
QRFAQASTLT YHVRRHTGEK PYVCDTCGKA FAVSSSLITH ARKHTGEKPY ICGVCRKSFI
SSGELNKHFR SHTGERPFVC EVCGNSYTDV KNLKKHKLKM HKGSEEAIEM KSAENSSSSE
DSTTKSPEPE SLELKPSDLF LPLTLHISPD DPQMLLPVSD NRGLSSETLL RASVPSYSEP
QFIFLQQMY