CSN5_DICDI
ID CSN5_DICDI Reviewed; 332 AA.
AC Q54PF3; Q2PQ74;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
GN Name=csn5; ORFNames=DDB_G0284597;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN THE CSN COMPLEX.
RX PubMed=16781008; DOI=10.1016/j.ejcb.2006.04.006;
RA Rosel D., Kimmel A.R.;
RT "The COP9 signalosome regulates cell proliferation of Dictyostelium
RT discoideum.";
RL Eur. J. Cell Biol. 85:1023-1034(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of E3 ligasew complexes, leading to modify the Ubl ligase
CC activity. In the complex, it probably acts as the catalytic center that
CC mediates the cleavage of Nedd8 from cullins. Csn5 is essential for
CC growth or survival.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the CSN complex. The holocomplex is comprised of
CC 8 subunits csn1-8. In the complex, it probably interacts directly with
CC csn1, csn2, csn3, csn4, csn6 and csn8. {ECO:0000269|PubMed:16781008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC CSN complex resulting in deneddylation of cullins. It constitutes the
CC catalytic center of the complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ309433; ABC46697.1; -; mRNA.
DR EMBL; AAFI02000069; EAL65137.1; -; Genomic_DNA.
DR RefSeq; XP_638491.1; XM_633399.1.
DR AlphaFoldDB; Q54PF3; -.
DR SMR; Q54PF3; -.
DR STRING; 44689.DDB0233103; -.
DR MEROPS; M67.A13; -.
DR PaxDb; Q54PF3; -.
DR EnsemblProtists; EAL65137; EAL65137; DDB_G0284597.
DR GeneID; 8624671; -.
DR KEGG; ddi:DDB_G0284597; -.
DR dictyBase; DDB_G0284597; csn5.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; Q54PF3; -.
DR OMA; ALWNKYW; -.
DR PhylomeDB; Q54PF3; -.
DR Reactome; R-DDI-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DDI-8951664; Neddylation.
DR PRO; PR:Q54PF3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0008180; C:COP9 signalosome; IPI:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0000338; P:protein deneddylation; IBA:GO_Central.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR Pfam; PF18323; CSN5_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW Reference proteome; Signalosome; Zinc.
FT CHAIN 1..332
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000327768"
FT DOMAIN 54..191
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 137..150
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 332 AA; 37889 MW; B08184F4CE6516AD CRC64;
MSKNGAADAL KTFELENNIQ TIDHDQLFKY DPQQYQQFLQ SKPWSKDPHY FKHVKISAIA
LLKMVMHARS GGKLEVMGML MGKVENNTMI IMDSFALPVE GTETRVNAQV EAYEYMVEYL
ELIKQTGRLE NALGWYHSHP GYGCWLSGID VGTQSVNQQY SEPWLGIVID PTRTVSAGKV
EIGAFRTYPQ GYKPPNEGPS EYQSIPLSKI EDFGVHCKQY YSLEITYFKS SLDQQLLDKL
WNKYWVNTLS SSPIFSNRDY ITGQINDLSE KLEQAETQLS HSRSSILDKK KEESLLSKVS
KDSSKVTIEQ VQGIMSQVFK NSIFNECQTT KQ
