ID   DTX1_XENLA              Reviewed;         623 AA.
AC   Q8AW93;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=E3 ubiquitin-protein ligase DTX1;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE   AltName: Full=Protein deltex-1;
DE            Short=xDtx1;
DE   AltName: Full=RING-type E3 ubiquitin transferase DTX1 {ECO:0000305};
GN   Name=dtx1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=12617815; DOI=10.1016/s0925-4773(02)00382-9;
RA   Andreazzoli M., Marracci S., Panattoni M., Nardi I.;
RT   "Xdtx1, a Xenopus Deltex homologue expressed in differentiating neurons and
RT   in photoreceptive organs.";
RL   Gene Expr. Patterns 2:283-287(2002).
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 vivo, mediating ubiquitination and
CC       promoting degradation of MEKK1, suggesting that it may regulate the
CC       Notch pathway via some ubiquitin ligase activity.
CC       {ECO:0000250|UniProtKB:Q61010}.
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: May form a homo- or heterodimer with other members of the
CC       Deltex family. Probably interacts with Notch1.
CC       {ECO:0000250|UniProtKB:Q86Y01}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in regions undergoing
CC       neuronal differentiation. Mainly colocalizes with Notch1.
CC   -!- DEVELOPMENTAL STAGE: In the tailbud stage, it is expressed in the
CC       olfactory bulbs, pineal complex and along the neural tube according to
CC       an antero-posterior gradient showing a gap at the midbrain-hindbrain
CC       boundary. At tadpole stage, it is expressed in the differentiating
CC       retina, in the neuronal fibers of the outer and inner plexiform layers,
CC       while its expression in the pineal complex becomes restricted to the
CC       photosensitive frontal organ. {ECO:0000269|PubMed:12617815}.
CC   -!- DOMAIN: The WWE domains are thought to mediate some protein-protein
CC       interaction, and are frequently found in ubiquitin ligases.
CC       {ECO:0000250|UniProtKB:Q86Y01}.
CC   -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
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DR   EMBL; AJ431211; CAD26517.1; -; mRNA.
DR   RefSeq; NP_001082450.1; NM_001088981.1.
DR   AlphaFoldDB; Q8AW93; -.
DR   SMR; Q8AW93; -.
DR   GeneID; 398477; -.
DR   KEGG; xla:398477; -.
DR   AGR; Xenbase:XB-GENE-865444; -.
DR   Xenbase; XB-GENE-865444; dtx1.L.
DR   OrthoDB; 5487971at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 398477; Expressed in camera-type eye and 5 other cell types or tissues.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; cd16671; RING-H2_DTX1_4; 1.
DR   Gene3D; 3.30.390.130; -; 1.
DR   Gene3D; 3.30.720.50; -; 2.
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; IPR004170; WWE-dom.
DR   InterPro; IPR018123; WWE-dom_subgr.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR   PANTHER; PTHR12622:SF7; E3 UBIQUITIN-PROTEIN LIGASE DTX1; 1.
DR   Pfam; PF18102; DTC; 1.
DR   Pfam; PF02825; WWE; 2.
DR   SMART; SM00678; WWE; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF117839; WWE domain; 2.
DR   PROSITE; PS50918; WWE; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Notch signaling pathway; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..623
FT                   /note="E3 ubiquitin-protein ligase DTX1"
FT                   /id="PRO_0000219082"
FT   DOMAIN          13..93
FT                   /note="WWE 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT   DOMAIN          94..170
FT                   /note="WWE 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT   ZN_FING         413..474
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          224..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  68333 MW;  0BBE3411882F8F36 CRC64;
     MSRPGVLLPV NGHNFGSQGG PPRVVVWEWL NEHGRWRPYT ATVCHHIENA LREDGRGRVA
     LGQVDAQLTP YVIDLQTMHQ YRQDTGTIRP VRRNFFEPSS APGKGIVWEW ENDAGSWTPY
     DTEICIAIQN AYEKHHPYLD LTTLGFCYLV HFHSMCQVNR QTHRKRRLRR RMDLAYPLTM
     GSIPKSQSWP VGSGSGLPCS CPQCLLVNST RAASNAILAS QRIKVPSGPP PALPPPPPPP
     IHPSGLRQSN TYSGGAAGWG RTGEGMRSTG GIRNGSGFSR SQSVPGAAPY PGQNNLNRPG
     EQRTSGSSSR ASIPPGVPAL PVKNLNGSGP VHPALAGMTG ILMCAAGLPV CLTRAPKPIL
     HPPPVSKEDI KPVSGVSGIC RKTKKKHLKK SKNPEEVVRR YIQKVKSPPD EDCTICMERL
     VTASGYDGVL SHRGIRAELV GKLGKCNHMY HVLCPVAMYN NGNKDGSLQC PTCKAIYGEK
     TGTQPPGKME FHVIPHSLPG FSDCKTIRIV YDIPSGMQGP EHPNPGKKFT ARGFPRHCYL
     PDNDKGRKVL RLLLAAWERR LIFAIGTSST TGESNTVVWN EIHHKTEFGS NLTGHGYPDP
     NYLDNVLTEL HRQGVMEERS LPY
//