DCNL4_DANRE
ID DCNL4_DANRE Reviewed; 280 AA.
AC Q5RHX6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DCN1-like protein 4;
DE Short=DCNL4 {ECO:0000250|UniProtKB:Q92564};
DE AltName: Full=DCUN1 domain-containing protein 4;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 4;
GN Name=dcun1d4 {ECO:0000250|UniProtKB:Q92564}; ORFNames=si:ch211-14g4.1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., 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).
CC -!- FUNCTION: Contributes to the neddylation of all cullins by transferring
CC NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to
CC different cullin C-terminal domain-RBX complexes.
CC {ECO:0000250|UniProtKB:Q92564}.
CC -!- SUBUNIT: May interact (via the DCUN1 domain) with unneddylated cullins.
CC {ECO:0000250|UniProtKB:Q92564}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92564}.
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, may mediate the
CC interaction with cullins. {ECO:0000250|UniProtKB:Q92564}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI11616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX323889; CAI11616.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5RHX6; -.
DR SMR; Q5RHX6; -.
DR STRING; 7955.ENSDARP00000114939; -.
DR PaxDb; Q5RHX6; -.
DR ZFIN; ZDB-GENE-041014-248; dcun1d4.
DR eggNOG; KOG3077; Eukaryota.
DR InParanoid; Q5RHX6; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR PRO; PR:Q5RHX6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:2000436; P:positive regulation of protein neddylation; ISS:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..280
FT /note="DCN1-like protein 4"
FT /id="PRO_0000129505"
FT DOMAIN 89..275
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 37..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 32421 MW; A0C354AACC15688C CRC64;
MHSDASNFQL NSHLSTLASI HKIYHTLHRL NLTEDVGPES HGTACCSRAM PPRKKRRPTA
GDDLSAKKSR QDNVYRKQEA LQIQEAEAFS SKRCLEWFYE YAGCDDVVGP EGMEKFCEDI
GVEPENVVML VLAWKLDAQS MGYFTLQEWL KGMGSLQCDS TEKLRNSLDY LRSVLNDATS
FKLIYRYAFD FAREKDQRSL DLNTAKCMLG LLLGKTWPLF PVFNQFLEQS KYKVINKDQW
CNVLEFSRTI NLDLSNYDED GAWPVLLDEF VEWYKDREMS
