DCNL3_BOVIN
ID DCNL3_BOVIN Reviewed; 304 AA.
AC Q5E9V1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 and may play a role in
CC the cell cycle progression by regulating the SCF ubiquitin E3 ligase
CC complex, after UV damage. At the cell membrane, can promote and as well
CC inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
CC -!- SUBUNIT: Part of a complex containing DCUN1D3, CUL3 and RBX1. Interacts
CC (via the DCUN1 domain) with the unneddylated cullins: interacts with
CC CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these interactions promote the
CC cullin neddylation and the identity of the cullin dictates the affinity
CC of the interaction. Interacts preferentially with CUL3; this
CC interaction triggers the relocalization of CUL3 to the cell membrane
CC where CUL3 is neddylated. Interacts (via DCUN1 domain) with RBX1. May
CC also interact with regulators or subunits of cullin-RING ligases such
CC as RNF7, ELOB and DDB1; these interactions are bridged by cullins.
CC Interacts (via DCUN1 domain) with CAND1; this interaction is bridged by
CC cullins and strongly inhibits cullin neddylation. These CAND-cullin-
CC DCNL complexes can only be neddylated in the presence of a substrate
CC adapter. Interacts (via DCUN1 domain) with the N-terminally acetylated
CC form of UBE2M and UBE2F. {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}. Note=After UVC treatment, the protein
CC enters to the nucleus gradually. Cell membrane localization is
CC essential for CUL3 neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins. The DCUN1 domain mediates the
CC interaction with the N-terminally acetylated NEDD8-conjugating E2s
CC enzyme leading to the NEDD8 transfer from N-terminally acetylated
CC NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX
CC complexes; the neddylation efficiency correlates with the DCUN1D5-
CC cullin and DCUN1D5-E2 interaction affinities. This domain is also
CC involved in CAND1-, cullins- and RBX1-binding.
CC {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; BT020819; AAX08836.1; -; mRNA.
DR RefSeq; NP_001015518.1; NM_001015518.1.
DR RefSeq; XP_005224760.1; XM_005224703.3.
DR RefSeq; XP_005224761.1; XM_005224704.3.
DR RefSeq; XP_005224765.1; XM_005224708.3.
DR RefSeq; XP_010817585.1; XM_010819283.2.
DR RefSeq; XP_015315801.1; XM_015460315.1.
DR RefSeq; XP_015315802.1; XM_015460316.1.
DR AlphaFoldDB; Q5E9V1; -.
DR SMR; Q5E9V1; -.
DR STRING; 9913.ENSBTAP00000043119; -.
DR PaxDb; Q5E9V1; -.
DR PRIDE; Q5E9V1; -.
DR Ensembl; ENSBTAT00000045756; ENSBTAP00000043119; ENSBTAG00000032260.
DR Ensembl; ENSBTAT00000079436; ENSBTAP00000072489; ENSBTAG00000032260.
DR GeneID; 504926; -.
DR KEGG; bta:504926; -.
DR CTD; 123879; -.
DR VEuPathDB; HostDB:ENSBTAG00000032260; -.
DR VGNC; VGNC:27937; DCUN1D3.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000154944; -.
DR HOGENOM; CLU_047042_2_0_1; -.
DR InParanoid; Q5E9V1; -.
DR OMA; ILDQWLH; -.
DR OrthoDB; 1418097at2759; -.
DR TreeFam; TF313332; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000032260; Expressed in spermatid and 107 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; ISS:UniProtKB.
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:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:2000435; P:negative regulation of protein neddylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; 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 GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0010225; P:response to UV-C; 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 CHAIN 2..304
FT /note="DCN1-like protein 3"
FT /id="PRO_0000320047"
FT DOMAIN 86..278
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
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 304 AA; 34304 MW; 6D8A7C43894922DD CRC64;
MGQCVTKCKN PSSTLGSKNG DRDPSSKSHG RRSASHREEQ LPTCGKPGGD ILVNGTKKAE
AAPEACQLPT SSGDAGREPK SNAEESSLQR LEELFRRYKD EREDAILEEG MERFCNDLCV
DPTEFRVLLL AWKFQAATMC KFTRKEFFDG CKAISADSID GICARFPSLL TEAKQEDKFK
DLYRFTFQFG LDSEEGQRSL HREIAIALWK LVFTQNNPPV LDQWLNFLTE NPSGIKGISR
DTWNMFLNFT QVIGPDLSNY SEDEAWPSLF DTFVEWEMER RKREGEGRGA LSSGPEGLCP
EEQT
