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DCNL5_RAT
ID   DCNL5_RAT               Reviewed;         237 AA.
AC   Q5PPL2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DCN1-like protein 5 {ECO:0000305};
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 {ECO:0000312|RGD:1307008};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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-41 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; BC087627; AAH87627.1; -; mRNA.
DR   RefSeq; NP_001009696.1; NM_001009696.1.
DR   AlphaFoldDB; Q5PPL2; -.
DR   SMR; Q5PPL2; -.
DR   STRING; 10116.ENSRNOP00000058633; -.
DR   jPOST; Q5PPL2; -.
DR   PaxDb; Q5PPL2; -.
DR   GeneID; 315405; -.
DR   KEGG; rno:315405; -.
DR   UCSC; RGD:1307008; rat.
DR   CTD; 84259; -.
DR   RGD; 1307008; Dcun1d5.
DR   VEuPathDB; HostDB:ENSRNOG00000008390; -.
DR   eggNOG; KOG3077; Eukaryota.
DR   HOGENOM; CLU_047042_3_1_1; -.
DR   InParanoid; Q5PPL2; -.
DR   OMA; HERKCKI; -.
DR   OrthoDB; 1418097at2759; -.
DR   PhylomeDB; Q5PPL2; -.
DR   TreeFam; TF354270; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   PRO; PR:Q5PPL2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008390; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q5PPL2; RN.
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..237
FT                   /note="DCN1-like protein 5"
FT                   /id="PRO_0000254174"
FT   DOMAIN          46..232
FT                   /note="DCUN1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTE7"
SQ   SEQUENCE   237 AA;  27568 MW;  63151DA73D85AB5A CRC64;
     MPVKKKRKAP GVAAAVAEDA GLKKCKISSY CRSQPPARLI SGEEDFSRKK CLAWFYEYAG
     PDEVVGPEGM EKFCEDIGVE PENIIMLVLA WKLEAESMGF FTKEEWLKGM TSLQCDCTEK
     LQSRFDFLRS QLNDISSFKN IYRYAFDFAR DKDQRSLDID TAKSMLALLL GRTWPLFSVF
     YQYLEQSKYR VMNKDQWYNV LEFSRTVHAD LSNYDEDGAW PVLLDEFVEW QKIRQTS
 
 
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