ID   A0A2U3YEH7_LEPWE        Unreviewed;       845 AA.
AC   A0A2U3YEH7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   28-JAN-2026, entry version 31.
DE   SubName: Full=E3 ubiquitin-protein ligase ZNF598 {ECO:0000313|RefSeq:XP_006742003.1};
GN   Name=ZNF598 {ECO:0000313|RefSeq:XP_006742003.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Monachinae; Lobodontini; Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006742003.1};
RN   [1] {ECO:0000313|RefSeq:XP_006742003.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006742003.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_006742003.1; XM_006741940.2.
DR   AlphaFoldDB; A0A2U3YEH7; -.
DR   STRING; 9713.A0A2U3YEH7; -.
DR   GeneID; 102737005; -.
DR   KEGG; lww:102737005; -.
DR   CTD; 90850; -.
DR   OrthoDB; 3838338at2759; -.
DR   Proteomes; UP000245341; Unplaced.
DR   GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR   InterPro; IPR057634; PAH_ZNF598/HEL2.
DR   InterPro; IPR056437; Znf-C2H2_ZNF598/HEL2.
DR   InterPro; IPR044288; ZNF598/HEL2.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR059042; Znf_C2H2_ZNF598.
DR   PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR   PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR   Pfam; PF23202; PAH_ZNF598; 1.
DR   Pfam; PF25447; RING_ZNF598; 1.
DR   Pfam; PF23230; zf-C2H2_13; 1.
DR   Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245341}.
FT   DOMAIN          124..145
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          248..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..266
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..364
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..440
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..481
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..607
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  92403 MW;  E3DD6F7F898D2CD8 CRC64;
     MGHPRRGLQV VFGKKLPAFA TIPLHQLQHE KKYDIYFADG KVFALYRQLL QHECPQCPEL
     PPFGLFGDLE QHMRKQHELF CCKLCLKHLK IFTYERKWYS RKDLARHRML GDPDDTSHRG
     HPLCKFCDER YLDNDELLKH LRRDHYFCHF CDSDGAQDYY SDYAYLREHF REKHFLCEEG
     RCSTEQFTHA FRTEIDLKAH RTACHSRSRA EARQNRQIDL QFSYAPRHSR RSEGVVGGED
     YEEVDRYNRQ GRAGRASGRG AQQNRRGSWR YKREEEDREV AAAIRASVAM QQPQQETRRS
     EDREEGSRAK KEEAGLRALE ELRGPRRLPR TQGEGAGLKE ASPNGPVSQE GLPATGPATG
     ATPPSTLPPP TSKLKDEDFP SLCASASFSS STLCSAAAAL GPVGLALAYP VPARGRSTFQ
     EDDFPALVSS ASKPSTAPTS LISAWNSSGS KKVAHPTPGA QTAGGSSQPP RKAGKGGKGS
     KKGAPPPSEE EEEDGRTGLT AQELRSVPTT VAVSSLLALA STHTLPKVGK KKKVGSEKPA
     AASPPPQPPD KDGPPGAEQA PTTTASRAEG PVALIVNGHT EGPAPARSTP KEPPGLPRPL
     GPPPCPTPQE DFPALGVPCP PRMPPPPGFN AVVLLKGTPP PPPPGLVPPV SKPPPGFSGL
     LPSPHPACVP STVTATKAPR LTPAPQAYLV PENFRERNLQ LIQSIKDFLQ SDEARFGKFK
     SHSGEFRQGV ISAAQYYKSC RDLLGENFQK IFNELLVLLP DTAKQQELLS AHTHFRGRER
     PPGAKAKKNR KSAWQANTRP AGLDCCVCPT CQQVLAHGDV SGHQALHAAQ DNDFPSLQAI
     ARILT
//