ID   DCNL3_XENTR             Reviewed;         303 AA.
AC   A4IHK8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DCN1-like protein 3 {ECO:0000250|UniProtKB:Q8IWE4};
DE            Short=DCNL3 {ECO:0000250|UniProtKB:Q8IWE4};
DE   AltName: Full=DCUN1 domain-containing protein 3;
DE   AltName: Full=Defective in cullin neddylation protein 1-like protein 3;
GN   Name=dcun1d3 {ECO:0000250|UniProtKB:Q8IWE4};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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. At the cell membrane,
CC       can promote and as well inhibit cullins neddylation.
CC       {ECO:0000250|UniProtKB:Q8IWE4}.
CC   -!- SUBUNIT: May interact (via the DCUN1 domain) with unneddylated cullins.
CC       {ECO:0000250|UniProtKB:Q8IWE4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8IWE4}.
CC   -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC       interaction with different cullins. {ECO:0000250|UniProtKB:Q8IWE4}.
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DR   EMBL; BC135572; AAI35573.1; -; mRNA.
DR   RefSeq; NP_001096288.1; NM_001102818.1.
DR   RefSeq; XP_012825425.1; XM_012969971.2.
DR   RefSeq; XP_017952510.1; XM_018097021.1.
DR   AlphaFoldDB; A4IHK8; -.
DR   SMR; A4IHK8; -.
DR   STRING; 8364.ENSXETP00000036490; -.
DR   PaxDb; A4IHK8; -.
DR   DNASU; 100124860; -.
DR   GeneID; 100124860; -.
DR   KEGG; xtr:100124860; -.
DR   CTD; 123879; -.
DR   Xenbase; XB-GENE-6258756; dcun1d3.
DR   eggNOG; KOG3077; Eukaryota.
DR   HOGENOM; CLU_047042_2_0_1; -.
DR   InParanoid; A4IHK8; -.
DR   OMA; TWQMFLN; -.
DR   OrthoDB; 1418097at2759; -.
DR   TreeFam; TF313332; -.
DR   Reactome; R-XTR-8951664; Neddylation.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000016729; Expressed in 4-cell stage embryo and 26 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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:2000435; P:negative regulation of protein neddylation; ISS:UniProtKB.
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   GO; GO:0010564; P:regulation of cell cycle process; ISS:UniProtKB.
DR   GO; GO:2000434; P:regulation of protein neddylation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Lipoprotein; Membrane; Myristate; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..303
FT                   /note="DCN1-like protein 3"
FT                   /id="PRO_0000320054"
FT   DOMAIN          85..277
FT                   /note="DCUN1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWE4, ECO:0000255"
SQ   SEQUENCE   303 AA;  34591 MW;  DF9199550EBB879F CRC64;
     MGQCVTKCKN PSSTLGSKNG ERESSKPHKR SSSHKDEHLS ICGKASREIL VNGTKKGDVS
     LEASQPLAAG GDTKKKEQGT GAELSSVQRI EELFWRYKDE REDAILEEGM ERFCNDLYVD
     PTEFRVLVLA WKFQAATMCK FTRREFFEGC KAINADGIEG ICARFPSLLN EAKQEDKFKD
     LYRFTFQFGL DSEEGQRSLH REIAIALWKL VFTQNKPLIL DQWLDFLTEN PSGIKGISRD
     TWNMFLNFTQ VIGPDLSNYS EDEAWPSLFD TFVEWEMERR KNEEETKCIP CSGTDDQSTE
     GQT