DCNL3_XENLA
ID DCNL3_XENLA Reviewed; 303 AA.
AC Q6DFA1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC076839; AAH76839.1; -; mRNA.
DR RefSeq; NP_001086584.1; NM_001093115.1.
DR AlphaFoldDB; Q6DFA1; -.
DR SMR; Q6DFA1; -.
DR DNASU; 446419; -.
DR GeneID; 446419; -.
DR KEGG; xla:446419; -.
DR CTD; 446419; -.
DR Xenbase; XB-GENE-6256234; dcun1d3.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 446419; Expressed in blastula and 19 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:0097602; F:cullin family protein binding; ISS:UniProtKB.
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: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_0000320053"
FT DOMAIN 85..277
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 1..40
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..40
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; 34627 MW; 7DD352CCB4848BB0 CRC64;
MGQCVTKCKN PSSTLGSKNG ERESSKPHKR SSSHKEEHMS ICGKASGEIL VNGTKKGDAS
LEASQPLAVG VDTKKKEQGV GAELSSLQRI EELFRRYKDE REDAILEEGM ERFCDDLCVD
PTEFRVLVLA WKFQAATMCK FTRREFFEGC KSINADGIES ICSQFPGLLN EAKQEDKFKD
LYRFTFQFGL DSEEGQRSLH REIAIALWKL VFTQNKPLIL DQWLEFLTEN PSGIKGISRD
TWNMFLNFTQ VIGPDLSNYS EDEAWPSLFD TFVEWEMERR KSEEKTDCIP CLGTDHQSRD
EQT