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Database: UniProt
Entry: A0AAD9FH62_DISEL
LinkDB: A0AAD9FH62_DISEL
Original site: A0AAD9FH62_DISEL 
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
//
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