DTX1_XENLA
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 03-AUG-2022, entry version 85.
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 CTD; 398477; -.
DR Xenbase; XB-GENE-865444; dtx1.L.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398477; Expressed in camera-type eye and 5 other 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 Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
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; PTHR12622; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF117839; SSF117839; 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