DCNL5_BOVIN
ID DCNL5_BOVIN Reviewed; 236 AA.
AC Q1RMX9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=DCN1-like protein 5 {ECO:0000250|UniProtKB:Q9BTE7};
DE AltName: Full=DCUN1 domain-containing protein 5;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 5;
DE AltName: Full=Squamous cell carcinoma-related oncogene 5 {ECO:0000250|UniProtKB:Q9BTE7};
GN Name=DCUN1D5;
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].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) 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 which is necessary for
CC the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a
CC role in DNA damage response and may participate in cell proliferation
CC and anchorage-independent cell growth. {ECO:0000250|UniProtKB:Q9BTE7}.
CC -!- SUBUNIT: Part of a complex that contains DCUN1D5, CUL1 and RBX1; this
CC interaction is bridged by CUL1. Interacts (via the DCUN1 domain) with
CC the unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B
CC and CUL5; these interactions promote the cullin neddylation and the
CC identity of the cullin dictates the affinity of the interaction.
CC Interacts (via DCUN1 domain) with UBE2M (N-terminally acetylated form)
CC and probably with UBE2F (N-terminally acetylated form). May also
CC interact with regulators or subunits of cullin-RING ligases such as
CC RBX1, RNF7, ELOB and DDB1; these interactions are bridged by cullins.
CC Interacts with CAND1; this interaction is bridged by cullins and
CC strongly inhibits the neddylation of cullins. These CAND-cullin-DCNL
CC complexes can only be neddylated in the presence of a substrate
CC adapter. {ECO:0000250|UniProtKB:Q9BTE7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTE7}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BTE7}.
CC Note=Subcellular localization is independent of the interaction with
CC cullins. {ECO:0000250|UniProtKB:Q9BTE7}.
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.
CC {ECO:0000250|UniProtKB:Q9BTE7}.
CC -!- PTM: Phosphorylation at Ser-40 is independent of cullin's interaction
CC and neddylation. Phosphorylated in response to both TICAM1 and MYD88
CC dependent Toll-like receptor (TLR) pathway activation (By similarity).
CC Phosphorylated in response to IL1B stimulation (By similarity).
CC {ECO:0000250|UniProtKB:Q9BTE7, ECO:0000250|UniProtKB:Q9CXV9}.
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DR EMBL; BC114644; AAI14645.1; -; mRNA.
DR RefSeq; NP_001039477.1; NM_001046012.1.
DR AlphaFoldDB; Q1RMX9; -.
DR SMR; Q1RMX9; -.
DR STRING; 9913.ENSBTAP00000004020; -.
DR PaxDb; Q1RMX9; -.
DR PRIDE; Q1RMX9; -.
DR Ensembl; ENSBTAT00000004020; ENSBTAP00000004020; ENSBTAG00000003087.
DR GeneID; 508759; -.
DR KEGG; bta:508759; -.
DR CTD; 84259; -.
DR VEuPathDB; HostDB:ENSBTAG00000003087; -.
DR VGNC; VGNC:27938; DCUN1D5.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000156155; -.
DR HOGENOM; CLU_047042_3_1_1; -.
DR InParanoid; Q1RMX9; -.
DR OMA; HERKCKI; -.
DR OrthoDB; 1418097at2759; -.
DR TreeFam; TF354270; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000003087; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; Q1RMX9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; 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:0006974; P:cellular response to DNA damage stimulus; 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:0001558; P:regulation of cell growth; 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 Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..236
FT /note="DCN1-like protein 5"
FT /id="PRO_0000254170"
FT DOMAIN 45..231
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE7"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE7"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE7"
SQ SEQUENCE 236 AA; 27362 MW; 34161CA67400B9C8 CRC64;
MPVKKKRKSG VAAAAAEDGG LKKCKISSYC RSQPPARLIS GEEHFSSKKC LAWFYEYAGP
DEVVGPEGME KFCEDIGVEP ENIIMLVLAW KLEAESMGFF TKEEWLKGMT SLQCDCTEKL
QNKFDFLRSQ LNDISSFKNI YRYAFDFARD KDQRSLDIDT AKSMLALLLG RTWPLFSVFY
QYLEQSKYRV MNKDQWYNVL EFSRTVHADL SNYDEDGAWP VLLDEFVEWH KVRQAS
