DCNL4_MOUSE
ID DCNL4_MOUSE Reviewed; 292 AA.
AC Q8CCA0; Q2YDW5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DCN1-like protein 4;
DE Short=DCNL4 {ECO:0000250|UniProtKB:Q92564};
DE AltName: Full=DCUN1 domain-containing protein 4;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 4;
GN Name=Dcun1d4 {ECO:0000312|MGI:MGI:2140972};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Olfactory epithelium;
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 are necessary
CC for the activation of cullin-RING E3 ubiquitin ligases (CRLs).
CC {ECO:0000250|UniProtKB:Q92564}.
CC -!- SUBUNIT: Interacts (via the DCUN1 domain) with the unneddylated
CC cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these
CC interactions promote the cullin neddylation and the identity of the
CC cullin dictates the affinity of the interaction. Interacts with RBX1
CC and RNF7. Interacts with CAND1; this interaction is bridged by cullins
CC such as CUL3 and strongly inhibits the neddylation of CUL3. These CAND-
CC cullin-DCNL complexes can only be neddylated in the presence of a
CC substrate adapter. Interacts (via DCUN1 domain) with UBE2M (N-
CC terminally acetylated form) and probably with UBE2F (N-terminally
CC acetylated form). {ECO:0000250|UniProtKB:Q92564}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92564}.
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:Q92564}.
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DR EMBL; AK033559; BAC28359.1; -; mRNA.
DR EMBL; BC108346; AAI08347.1; -; mRNA.
DR EMBL; BC137627; AAI37628.1; -; mRNA.
DR EMBL; BC137628; AAI37629.1; -; mRNA.
DR CCDS; CCDS19342.1; -.
DR RefSeq; NP_001177662.1; NM_001190733.1.
DR RefSeq; NP_001177663.1; NM_001190734.1.
DR RefSeq; NP_849227.1; NM_178896.5.
DR AlphaFoldDB; Q8CCA0; -.
DR SMR; Q8CCA0; -.
DR STRING; 10090.ENSMUSP00000067616; -.
DR iPTMnet; Q8CCA0; -.
DR PhosphoSitePlus; Q8CCA0; -.
DR MaxQB; Q8CCA0; -.
DR PaxDb; Q8CCA0; -.
DR PRIDE; Q8CCA0; -.
DR ProteomicsDB; 279391; -.
DR Antibodypedia; 23882; 110 antibodies from 17 providers.
DR DNASU; 100737; -.
DR Ensembl; ENSMUST00000063882; ENSMUSP00000067616; ENSMUSG00000051674.
DR GeneID; 100737; -.
DR KEGG; mmu:100737; -.
DR UCSC; uc008xsz.2; mouse.
DR CTD; 23142; -.
DR MGI; MGI:2140972; Dcun1d4.
DR VEuPathDB; HostDB:ENSMUSG00000051674; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000156935; -.
DR HOGENOM; CLU_047042_3_1_1; -.
DR InParanoid; Q8CCA0; -.
DR OMA; DEELAWP; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q8CCA0; -.
DR TreeFam; TF354270; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 100737; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Dcun1d4; mouse.
DR PRO; PR:Q8CCA0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CCA0; protein.
DR Bgee; ENSMUSG00000051674; Expressed in spermatid and 236 other tissues.
DR ExpressionAtlas; Q8CCA0; baseline and differential.
DR Genevisible; Q8CCA0; MM.
DR GO; GO:0005634; C:nucleus; 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: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 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 Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..292
FT /note="DCN1-like protein 4"
FT /id="PRO_0000129504"
FT DOMAIN 102..287
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 40..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92564"
SQ SEQUENCE 292 AA; 33939 MW; A599872179813601 CRC64;
MHSDAAAVNF QLNSHLSTLA SIHKIYHTLN KLNLTEDVGQ DDHQTGSLRS CSSSDCFSKV
MPPRKKRRPA SGDDLSAKKS RHDSMYRKYE STRIKTEEEA FSSKRCLEWF YEYAGTEDAV
GPEGMEKFCE DIGVEPENVV MLVLAWKLDA QNMGYFTLQE WLKGMTSLQC DTTEKLRTTL
DYLRSLLNDT TNFKLIYRYA FDFAREKDQR SLDINTAKCM LGLLLGKIWP LFPVFHQFLE
QSKYKVINKD QWCNVLEFSR TISLDLSNYD EDGAWPVLLD EFVEWYKDKQ MS
