ID A0A8C4L9L3_EQUAS Unreviewed; 922 AA.
AC A0A8C4L9L3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=ZNF598 {ECO:0000313|Ensembl:ENSEASP00005006303.2};
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005006303.2, ECO:0000313|Proteomes:UP000694387};
RN [1] {ECO:0000313|Ensembl:ENSEASP00005006303.2, ECO:0000313|Proteomes:UP000694387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33293529;
RA Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA S., Zhou, X. and Zhong, J.;
RT "Donkey genomes provide new insights into domestication and selection for
RT coat color.";
RL Nat. Commun. 11:6014-6014(2020).
RN [2] {ECO:0000313|Ensembl:ENSEASP00005006303.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSEASP00005006303.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR RefSeq; XP_044602858.1; XM_044746923.2.
DR AlphaFoldDB; A0A8C4L9L3; -.
DR Ensembl; ENSEAST00005006893.2; ENSEASP00005006303.2; ENSEASG00005004666.2.
DR GeneID; 106836274; -.
DR KEGG; eai:106836274; -.
DR CTD; 90850; -.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694387; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_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 InterPro; IPR001841; Znf_RING.
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; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694387};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 28..68
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 271..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..404
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..519
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..560
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 100821 MW; EE468D00768D35C7 CRC64;
MAAAAGTEGR RAALEAAAAV PERGGGSCVL CCGDLEATAL GRCDHPVCYR CSTKMRVLCE
QRYCAVCREE LRQVVFGKKL PAFATIPIHQ LQHEKKYDIY FADGKVFALY RQLLQHECPR
CPELPPFGLF GDLEQHMRKQ HELFCCKLCL KHLKIFTYER KWYSRKDLAR HRMQGDPDDT
SHRGHPLCKF CDERYLDNDE LLKHLRRDHY FCHFCDSDGA QDYYSDYAYL REHFREKHFL
CEEGRCSTEQ FTHAFRTEID LKAHRTACHS RSRAEARQNR QIDLQFSYTP RHSRRNEGVV
GGEDYEEVDR YNRQGRVGRA SGRGAQQSRR GSWRYKREEE DREVAAAIRA SVAAQQQQQQ
EARRSEDREE GGRLKKEEAG ARGTEEPRGP RRPPRTQGEG PGEQTLPAGS SAQASKHLGV
PKEATANGPV SQEAFPANSL ASGATLPSTL PPPTSELKDE DFPSLCASTS SSCSAAAALG
PVGLALVYPV PTRGRSTFQE DDFPALVSSA SKPSTAPTSL ISAWNSSSSK KVAHPTLGAQ
AASGGSQPPR KAGKGGKGGK KGGPPPVEEE EDGEEDGYAG RTTQELRSVP TTVAVSSLLA
LASTQTVTKV GKKKKVGSEK PGATPPPPLP PDKDGPPGGE QAPTGRAEGP VAVIVNGHTE
GPAPARNIPK EPPGLPRPLG PLPCPTPQED FPALGGPCPP RMPPPPGFNT VVLLKGTPPP
PPPGLVPAIS KPPPGFSSLL PSPHSACIPT TTTTTKVLTP VPRAYLVPEN FRERNLQLIQ
SIKDFLQSDE ARFSKFKSHS GEFRQGMISA AQYYKSCRDL LGENFQKIFN ELLVLLPDTT
KQQELLSAHT DFCGRERPPG TKAKKNKKSA WQTSTRQMGL DCCVCPACQQ VLAHGDVSSH
QALHAARDDD FPSLQAITRI LT
//
