ID A0AAD9FH62_DISEL Unreviewed; 986 AA.
AC A0AAD9FH62;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Zinc finger MIZ domain containing protein 1 {ECO:0000313|EMBL:KAK1905763.1};
GN ORFNames=KUDE01_012942 {ECO:0000313|EMBL:KAK1905763.1};
OS Dissostichus eleginoides (Patagonian toothfish) (Dissostichus amissus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=100907 {ECO:0000313|EMBL:KAK1905763.1, ECO:0000313|Proteomes:UP001228049};
RN [1] {ECO:0000313|EMBL:KAK1905763.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE {ECO:0000313|EMBL:KAK1905763.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1905763.1};
RA Park H.;
RT "Chromosome-level genome of Chaenocephalus aceratus.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK1905763.1}.
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DR EMBL; JASDAP010000003; KAK1905763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD9FH62; -.
DR Proteomes; UP001228049; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061665; F:SUMO ligase activity; IEA:TreeGrafter.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR GO; GO:0016925; P:protein sumoylation; IEA:TreeGrafter.
DR FunFam; 3.30.40.10:FF:000012; Zinc finger MIZ domain-containing protein 2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR057847; ZMIZ1/ZMIZ2_GBD-like.
DR InterPro; IPR040797; ZMIZ1_N.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10782:SF7; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF25527; GBD-like_ZMIZ1_ZMIZ2; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR Pfam; PF18028; Zmiz1_N; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 4: Predicted;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001228049};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 656..737
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 116..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..256
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..334
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..417
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..428
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..814
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..986
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 107098 MW; 03D605F887996952 CRC64;
MNTLPSMDRH IQQTNDRLLC IKQHLQNPAN FHSAATELLD WCGDPRAFQR PFEQSLMGCL
TVVSRVAAQQ GYDLDLGYRV LAVCAANRDK FTPKSAALLS SWCEELGRLL LLRHQKSRQN
EPQGKVPMQP SMNSMKPGLT HSDGSFPYDS VPWQQNTNQP PGSLSVVTTV WGVTNTSQSQ
VLGNHMANSN NPMNPGGNPM GSGMSASAGG MNSPQFNAQQ QQFPNKGGSN QQYMQQGMYG
RPGYPGGPGG YSGNYSGGPN PPQGGMGMTS HSRTPDMNQY GQMCSSFQMG PTQTYNSQFM
NQPGPRGPPG GMNPANMGSG MNNPNMSGPP MGMNQARTPG MVPFGAHGQR MPQQGYPGGP
RQGMPMQGMK RPYPGEASYG GQQYGPNGQQ GQGQYPPGMP MGQYYKQEPF NGQSNSFSGG
GYSYGQGNGP PRPVNYPHSP VPGNPTPPMT PGSSIPPYLS PNQDVKPPFP PDMKPNMTAL
PPPPSHPNEE LRLTFPVRDG VVLEPFRLEH NLAVSNHVFH LRPSVHQTLM WRSDLELQFK
CYHHEDRQMN TNWPASVQVS VNATPLTIER GDNKTSHKPL HLKQVCQPGR NTIQITVTAC
CCSHLFVLQL VHRPSVRSVL QGLLKKRLLP AEHCITKVKR NFSSVAASTG STTLNGEDGV
EQTAIKVSLK CPITFRRIQL PARGHDCKHV QCFDLESYLQ LNCERGTWRC PVCNKTALLE
GLEVDQYMWG VLNAIQNSEF EEVTIDPTCS WRPVPIKSDL HIKEDPDGPL AKRFKTMSPS
QMTMPNVMEM IAQLGPGSGP GPLLGPSPYP PHPSQHPSGN GGDYPGAGHT YHSQVSFDFP
HGNPSGVGGG GGPPMNDFIH APQLSHPPDG PGGLLSQDKP LNHGMNDAMS HTDQSHNSMQ
QSLHASPHPG SQSGLPLHHS GQSGPPLHHS GHDLNFNPSS DGQDMPEPSL DLLPELANPE
ELLSYLDPPD LPSNSNDDLL SLFENN
//