ID DTX3_PONAB Reviewed; 347 AA.
AC Q5REG4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Probable E3 ubiquitin-protein ligase DTX3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE AltName: Full=Protein deltex-3;
DE Short=Deltex3;
DE AltName: Full=RING-type E3 ubiquitin transferase DTX3 {ECO:0000305};
GN Name=DTX3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of Notch signaling, a signaling pathway involved in
CC cell-cell communications that regulates a broad spectrum of cell-fate
CC determinations. Probably acts both as a positive and negative regulator
CC of Notch, depending on the developmental and cell context. Functions as
CC a ubiquitin ligase protein in vitro, suggesting that it may regulate
CC the Notch pathway via some ubiquitin ligase activity. {ECO:0000250}.
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:0000250|UniProtKB:Q61010};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. May form a heterodimer with other members of the
CC Deltex family. Interacts with NOTCH1. {ECO:0000250|UniProtKB:Q80V91}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
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DR EMBL; CR857565; CAH89843.1; -; mRNA.
DR RefSeq; NP_001124856.1; NM_001131384.1.
DR AlphaFoldDB; Q5REG4; -.
DR SMR; Q5REG4; -.
DR Ensembl; ENSPPYT00000005559.3; ENSPPYP00000005350.3; ENSPPYG00000004697.3.
DR GeneID; 100171717; -.
DR KEGG; pon:100171717; -.
DR eggNOG; ENOG502QUYA; Eukaryota.
DR GeneTree; ENSGT00940000161404; -.
DR InParanoid; Q5REG4; -.
DR OMA; XAEHPNP; -.
DR OrthoDB; 5487971at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd09633; Deltex_C; 1.
DR CDD; cd16711; RING-HC_DTX3; 1.
DR Gene3D; 3.30.390.130; -; 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; 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:SF36; E3 UBIQUITIN-PROTEIN LIGASE DTX3-RELATED; 1.
DR Pfam; PF18102; DTC; 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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Notch signaling pathway; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="Probable E3 ubiquitin-protein ligase DTX3"
FT /id="PRO_0000307379"
FT ZN_FING 164..205
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 113..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 37988 MW; FDB4CDC982F1B707 CRC64;
MSFVLSRMAA CGGTCKNKVT VSKPVWDFLS KETPARLARL REEHRVSILI DGETSDIYVL
QLSPQGPPPA PPNGLYLARK ALKGLLKEAE KELKKAQRQG ELMGCLALGG GGEHPEMHRA
GPPPLRAAPL LPPGARGLPP PPPPLPPPLP PRLREEAEEQ ESTCPICLGE IQNAKTLEKC
RHSFCEGCIT RALQVKKACP MCGRFYGQLV GNQPQNGRML VSKDATLLLP SYEKYGTIVI
QYVFPPGVQG AEHPNPGVRY PGTTRVAYLP DCPEGNKVLT LFRKAFDQRL TFTIGTSMTT
GRPNVITWND IHHKTSCTGG PQLFGYPDPT YLTRVQEELR AKGITDD
//
