ID A0A493T4K6_ANAPP Unreviewed; 741 AA.
AC A0A493T4K6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN Name=DTX3L {ECO:0000313|Ensembl:ENSAPLP00000020570.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000020570.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000020570.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000020570.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR AlphaFoldDB; A0A493T4K6; -.
DR STRING; 8840.ENSAPLP00000020570; -.
DR Ensembl; ENSAPLT00000020405.1; ENSAPLP00000020570.1; ENSAPLG00000031101.1.
DR GeneTree; ENSGT00940000154578; -.
DR OMA; EYFKYIC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016666; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0141000; F:histone H4K91 ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140768; F:protein ADP-ribosyltransferase-substrate adaptor activity; IEA:Ensembl.
DR GO; GO:0097677; F:STAT family protein binding; IEA:Ensembl.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:Ensembl.
DR GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:2000646; P:positive regulation of receptor catabolic process; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd09633; Deltex_C; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR048418; DTX3L_a/b_dom.
DR InterPro; IPR048409; DTX3L_KH-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF41; E3 UBIQUITIN-PROTEIN LIGASE DTX3L; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF21717; DTX3L_a-b; 1.
DR Pfam; PF21718; DTX3L_KH-like; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 562..601
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 83..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 83469 MW; D2601EEDF6304FCA CRC64;
MAAPLLVKLS PAPDDSEKAK LKLQSYFQSG KRSGGGECEL QAGPEPGTFL VYFHQERDKK
NVESRTDHVV EMGAKCLKVS IQPEKGGLSG DQSTSQAAAS CSQPYHISPP PRGSREKQAA
EGQRDTAAET VTKKIFLTVS AILNTSMFTK QQREKIALVC PNLKREGNPD VDGYEKLTGD
YTDIEKAYHY FKDILAGYDQ HHDFSHTGSK NGLEDGNGLK NEESDELTVP SALYEYFCHT
CKDQIKELNE CFGVHLRNKD CNNGYISVCF NSNKSSRSSA SMQKAKDFFT SAFQKNIKDV
QQEKISLTNS YQLNETIMKL NNRFSNLLAK QEENQLLLRG PTKEILNAKN FLEEEMQNSQ
TEKNVDIPCE LYTYRNEIAV DASVFNLLET ALQKEIEDIK ENFDTVMEKK HSSDSQKMLI
IFKPRSKISD RFSHAIEAFI NAFQNAFAML REKLISCKLS EYQEQRLNML DGKQLEDLHV
KFKKKEDKII LYGLPNHLDA AEKHIMKLLN AGGSAETKTR TPLGNKEATG VSEKKYGDRQ
KSSFCSKEEA KAKTEEDTDS TCPICMEGMN DKVILTKCKH AFCRVCITKA MTYKKTCPVC
NTVYGPMQGN QPEGEMSFQF TRSCLPGYPN CGTIVIHYDM KGGIQTKDHP NPGAPYQAVF
RTAYLPNNKE GQEILQLLKR AFQQKLIFTV GQSRTTGLQG VITWNDIHHK TSIYGGPTNF
GYPDPDYLKR VRSELKARGI E
//
