CSN5_YEAST
ID CSN5_YEAST Reviewed; 440 AA.
AC Q12468; D6VRD8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=RRI1; Synonyms=CSN5, JAB1; OrderedLocusNames=YDL216C; ORFNames=D0888;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION OF THE COP9 SIGNALOSOME COMPLEX.
RX PubMed=12186635; DOI=10.1186/1471-2156-3-15;
RA Wee S., Hetfeld B., Dubiel W., Wolf D.A.;
RT "Conservation of the COP9/signalosome in budding yeast.";
RL BMC Genet. 3:15-15(2002).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH CSN12, IDENTIFICATION IN THE COP9
RP SIGNALOSOME COMPLEX, AND FUNCTION OF THE COP9 SIGNALOSOME-LIKE COMPLEX.
RX PubMed=12446563; DOI=10.1093/embo-reports/kvf235;
RA Maytal-Kivity V., Piran R., Pick E., Hofmann K., Glickman M.H.;
RT "COP9 signalosome components play a role in the mating pheromone response
RT of S. cerevisiae.";
RL EMBO Rep. 3:1215-1221(2002).
RN [6]
RP INTERACTION WITH CSN9; RRI2; PCI8; CSN12; CSI1 AND RPN5, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT protein complexes.";
RL Nature 415:141-147(2002).
RN [7]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-164; HIS-166 AND ASP-177.
RX PubMed=12183637; DOI=10.1126/science.1075901;
RA Cope G.A., Suh G.S.B., Aravind L., Schwarz S.E., Zipursky S.L.,
RA Koonin E.V., Deshaies R.J.;
RT "Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8
RT from Cul1.";
RL Science 298:608-611(2002).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH CSN12, AND IDENTIFICATION IN THE
RP COP9 SIGNALOSOME COMPLEX.
RX PubMed=12672462; DOI=10.1016/s1357-2725(02)00378-3;
RA Maytal-Kivity V., Pick E., Piran R., Hofmann K., Glickman M.H.;
RT "The COP9 signalosome-like complex in S. cerevisiae and links to other PCI
RT complexes.";
RL Int. J. Biochem. Cell Biol. 35:706-715(2003).
RN [9]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
CC -!- FUNCTION: Catalytic component of the COP9 signalosome (CSN) complex
CC that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by
CC mediating the deneddylation of the cullin subunit of SCF-type E3
CC ubiquitin-protein ligase complexes (By similarity). The CSN complex is
CC involved in the regulation of the mating pheromone response.
CC {ECO:0000250, ECO:0000269|PubMed:12183637, ECO:0000269|PubMed:12186635,
CC ECO:0000269|PubMed:12446563}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a COP9 signalosome-like (CSN) complex, composed
CC of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1.
CC Within this complex it probably interacts directly with CSN12. Also
CC interacts with RPN5. {ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:12446563, ECO:0000269|PubMed:12672462}.
CC -!- INTERACTION:
CC Q12468; Q04368: CSI1; NbExp=3; IntAct=EBI-37511, EBI-28044;
CC Q12468; P47130: CSN12; NbExp=3; IntAct=EBI-37511, EBI-763;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear localization
CC requires the formation of the CSN complex.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67474.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA98794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X99000; CAA67474.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74264; CAA98794.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA11648.1; -; Genomic_DNA.
DR PIR; S67775; S67775.
DR RefSeq; NP_010065.2; NM_001180276.1.
DR AlphaFoldDB; Q12468; -.
DR SMR; Q12468; -.
DR BioGRID; 31829; 176.
DR ComplexPortal; CPX-1894; COP9 signalosome complex.
DR DIP; DIP-1809N; -.
DR IntAct; Q12468; 8.
DR MINT; Q12468; -.
DR STRING; 4932.YDL216C; -.
DR iPTMnet; Q12468; -.
DR MaxQB; Q12468; -.
DR PaxDb; Q12468; -.
DR PRIDE; Q12468; -.
DR EnsemblFungi; YDL216C_mRNA; YDL216C; YDL216C.
DR GeneID; 851310; -.
DR KEGG; sce:YDL216C; -.
DR SGD; S000002375; RRI1.
DR VEuPathDB; FungiDB:YDL216C; -.
DR eggNOG; KOG1554; Eukaryota.
DR GeneTree; ENSGT00550000074850; -.
DR HOGENOM; CLU_031199_1_0_1; -.
DR InParanoid; Q12468; -.
DR OMA; QMESYEY; -.
DR BioCyc; YEAST:G3O-29597-MON; -.
DR PRO; PR:Q12468; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12468; protein.
DR GO; GO:0008180; C:COP9 signalosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
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; IMP:SGD.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0070452; P:positive regulation of ergosterol biosynthetic process; IMP:SGD.
DR GO; GO:0000338; P:protein deneddylation; IMP:SGD.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF6; PTHR10410:SF6; 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..440
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194859"
FT DOMAIN 71..218
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..177
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 319..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MUTAGEN 164
FT /note="H->A: Abolishes deneddylation of CDC53."
FT /evidence="ECO:0000269|PubMed:12183637"
FT MUTAGEN 166
FT /note="H->A: Abolishes deneddylation of CDC53."
FT /evidence="ECO:0000269|PubMed:12183637"
FT MUTAGEN 177
FT /note="D->A: Abolishes deneddylation of CDC53."
FT /evidence="ECO:0000269|PubMed:12183637"
SQ SEQUENCE 440 AA; 50812 MW; 56714AD214C32D36 CRC64;
MSLSNKTVKE LRQLLKERYT VEDELTESIA LSSMRFKPSQ EPEFHALSQS SLLKTKLKQQ
SSTDIPSYTH VLISKLSCEK ITHYAVRGGN IEIMGILMGF TLKDNIVVMD CFNLPVVGTE
TRVNAQLESY EYMVQYIDEM YNHNDGGDGR DYKGAKLNVV GWFHSHPGYD CWLSNIDIQT
QDLNQRFQDP YVAIVVDPLK SLEDKILRMG AFRTIESKSD DNSATSYYEL ETIIFDSELN
RALFETKLNL HCVIEDDESE QISLNRLIDS MKQYSYLMDS KNVRTRIKLA TTSERVSNEN
KKNIDYQNRS TRSQFCLNTQ RGDSTETSSF GSMFSGDNTS DVDMEDRNLT EFDSTDTSLC
INGEPSIHVN RVERSSRSTD NFHNSKKRMN SNQERCHDEG NDMLQRNVLE TDYARAKNRI
LASKIKQYER LRFYKDTFTL
