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Database: UniProt
Entry: B2KJ26_DANRE
LinkDB: B2KJ26_DANRE
Original site: B2KJ26_DANRE 
ID   B2KJ26_DANRE            Unreviewed;       704 AA.
AC   B2KJ26;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN   Name=dtx1 {ECO:0000313|EMBL:ABF61770.1,
GN   ECO:0000313|RefSeq:NP_001120780.1};
GN   Synonyms=si:ch211-119e14.2 {ECO:0000313|RefSeq:NP_001120780.1};
GN   OrderedLocusNames=dtx4a {ECO:0000313|RefSeq:NP_001120780.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-160728-59};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:ABF61770.1};
RN   [1] {ECO:0000313|EMBL:ABF61770.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wee I.X., Tan S.C.C., Xu H., Jiang Y.-J.;
RT   "Cloning and expression pattern of three zebrafish deltex genes.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_001120780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22538478;
RA   Blackburn J.S., Liu S., Raiser D.M., Martinez S.A., Feng H., Meeker N.D.,
RA   Gentry J., Neuberg D., Look A.T., Ramaswamy S., Bernards A., Trede N.S.,
RA   Langenau D.M.;
RT   "Notch signaling expands a pre-malignant pool of T-cell acute lymphoblastic
RT   leukemia clones without affecting leukemia-propagating cell frequency.";
RL   Leukemia 26:2069-2078(2012).
RN   [3] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_001120780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26714454; DOI=10.1186/s13064-015-0055-5;
RA   Cheng Y.C., Huang Y.C., Yeh T.H., Shih H.Y., Lin C.Y., Lin S.J., Chiu C.C.,
RA   Huang C.W., Jiang Y.J.;
RT   "Deltex1 is inhibited by the Notch-Hairy/E(Spl) signaling pathway and
RT   induces neuronal and glial differentiation.";
RL   Neural Dev. 10:28-28(2015).
RN   [5] {ECO:0000313|RefSeq:NP_001120780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [6] {ECO:0000313|RefSeq:NP_001120780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28631837;
RA   Shi W.J., Zhao J.L., Jiang Y.X., Huang G.Y., Liu Y.S., Zhang J.N.,
RA   Ying G.G.;
RT   "Transcriptional and histological alterations in gonad of adult zebrafish
RT   after exposure to the synthetic progestin norgestrel.";
RL   Environ. Toxicol. Chem. 36:3267-3276(2017).
RN   [7] {ECO:0000313|RefSeq:NP_001120780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [8] {ECO:0000313|RefSeq:NP_001120780.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   EMBL; DQ497599; ABF61770.1; -; mRNA.
DR   RefSeq; NP_001120780.1; NM_001127308.1.
DR   GeneID; 570481; -.
DR   KEGG; dre:570481; -.
DR   CTD; 570481; -.
DR   ZFIN; ZDB-GENE-160728-59; dtx4a.
DR   OrthoDB; 5487971at2759; -.
DR   PhylomeDB; B2KJ26; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000437; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR   PANTHER; PTHR12622:SF5; E3 UBIQUITIN-PROTEIN LIGASE DTX4; 1.
DR   Pfam; PF18102; DTC; 1.
DR   Pfam; PF02825; WWE; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
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   Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367105};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          1..78
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          79..155
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          494..555
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          232..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..250
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..322
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  75113 MW;  6D898AFF542ABB69 CRC64;
     MLLASAVVVW EWLNEHGRWR PYSPAVSHHI EAVIRSDPRG AGSVVLGQVD SRLSPYIIDL
     QSMHQFRQDT GTLRPVRRSF YDPRSAPGQG WVWEWENDSG SWTPYDTEVS IAIQAARDRQ
     QPWLDLTPLG FCYLIDLQSM TQINGQTQRR RRIQRRSDLA YPLVSGPLPK PHAWSSAGSG
     GLLGVGVSGV SGGNGSAYPS GALPASAITS LGQPCSCQQC MLVLGVKTPS MAQTLGRKPP
     PIPKPPSPKA PSRGHSYSLT LPHPPSLSRV LSPHRNSTSG ASGGFGHSLS LLGSATAALS
     ISSNRPPPPT VPPPPPPSTT PHTTSMANPT APTPSSTLIS TATTCAPTPS ARVLGPVSTA
     SAACAAPVPP CSSLAGLSRP ALQRIAMAQS RALIASGVPT VPVKNLNGSS PVHPALAGIT
     GILMSAAGLP VCLTRPPKLV LHPPPVSKSD IKPVPGLGHC CRKTTKKQAR KGRTSEEVVR
     RYLQKVRNPP EEDCTICMES LCGPSGYKGP GVGGISRAES VGRLSQCGHQ YHLQCLVAMY
     NNGNKDGSLQ CPTCKTIYGV KTGNQPPGKM EYHVIPHSLP GHPDCKTIRI IYNIPPGIQG
     PEHPNPGKPF TARGFPRHCY LPDSEKGRLV LKLLLVAWDR RLIFSVGTSS TTGETDTVIW
     NEVHHKTEFG SNLTGHGYPD SGHLDNVLKE LRAQGITEEE CLRD
//
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