CSN5A_ARATH
ID CSN5A_ARATH Reviewed; 357 AA.
AC Q8LAZ7; A1A6G7; F4I325; O23130; O82524; Q84WE7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=COP9 signalosome complex subunit 5a;
DE Short=Signalosome subunit 5a;
DE EC=3.4.-.-;
DE AltName: Full=Jun activation domain-binding homolog 1;
GN Name=CSN5A {ECO:0000303|PubMed:23424245};
GN Synonyms=AJH1 {ECO:0000303|PubMed:9811788},
GN CSN5B {ECO:0000303|PubMed:11742986};
GN OrderedLocusNames=At1g22920 {ECO:0000312|Araport:AT1G22920};
GN ORFNames=F19G10.12 {ECO:0000312|EMBL:AAB72159.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND SUBUNIT.
RC TISSUE=Seedling;
RX PubMed=9811788; DOI=10.2307/3870903;
RA Kwok S.F., Solano R., Tsuge T., Chamovitz D.A., Ecker J.R., Matsui M.,
RA Deng X.-W.;
RT "Arabidopsis homologs of a c-Jun coactivator are present both in monomeric
RT form and in the COP9 complex, and their abundance is differentially
RT affected by the pleiotropic cop/det/fus mutations.";
RL Plant Cell 10:1779-1790(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11742986; DOI=10.1093/emboj/20.24.7096;
RA Fu H., Reis N., Lee Y., Glickman M.H., Vierstra R.;
RT "Subunit interaction maps for the regulatory particle of the 26S proteasome
RT and the COP9 signalosome.";
RL EMBO J. 20:7096-7107(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Park D., Nam H.-G.;
RT "cDNA sequence for human JAB1 homolog from Arabidopsis thaliana (L.).";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-357 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [9]
RP FUNCTION.
RX PubMed=11337587; DOI=10.1126/science.1059776;
RA Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT SCF(TIR1) in mediating auxin response.";
RL Science 292:1379-1382(2001).
RN [10]
RP INTERACTION WITH CSN4 AND CSN6.
RX PubMed=12615944; DOI=10.1105/tpc.009092;
RA Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.-W.;
RT "Characterization of the last subunit of the Arabidopsis COP9 signalosome:
RT implications for the overall structure and origin of the complex.";
RL Plant Cell 15:719-731(2003).
RN [11]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-142; HIS-144; CYS-149; ASP-155
RP AND ASP-175.
RX PubMed=15486099; DOI=10.1105/tpc.104.025999;
RA Gusmaroli G., Feng S., Deng X.W.;
RT "The Arabidopsis CSN5A and CSN5B subunits are present in distinct COP9
RT signalosome complexes, and mutations in their JAMM domains exhibit
RT differential dominant negative effects on development.";
RL Plant Cell 16:2984-3001(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15923347; DOI=10.1105/tpc.105.032870;
RA Dohmann E.M., Kuhnle C., Schwechheimer C.;
RT "Loss of the CONSTITUTIVE PHOTOMORPHOGENIC9 signalosome subunit 5 is
RT sufficient to cause the cop/det/fus mutant phenotype in Arabidopsis.";
RL Plant Cell 17:1967-1978(2005).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17307927; DOI=10.1105/tpc.106.047571;
RA Gusmaroli G., Figueroa P., Serino G., Deng X.W.;
RT "Role of the MPN subunits in COP9 signalosome assembly and activity, and
RT their regulatory interaction with Arabidopsis Cullin3-based E3 ligases.";
RL Plant Cell 19:564-581(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP INTERACTION WITH CYT1.
RX PubMed=23424245; DOI=10.1105/tpc.112.106880;
RA Wang J., Yu Y., Zhang Z., Quan R., Zhang H., Ma L., Deng X.W., Huang R.;
RT "Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid
RT synthesis.";
RL Plant Cell 25:625-636(2013).
CC -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes such as photomorphogenesis and auxin and jasmonate responses.
CC The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of the SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF. In the complex, it probably acts as the
CC catalytic center that mediates the cleavage of Nedd8 from cullins. It
CC however has no metalloprotease activity by itself and requires the
CC other subunits of the CSN complex (By similarity). The CSN complex is
CC involved in repression of photomorphogenesis in darkness by regulating
CC the activity of COP1-containing Ubl ligase complexes. The complex is
CC also required for degradation of PSIAA6 by regulating the activity of
CC the Ubl ligase SCF-TIR complex. Involved in CSN's
CC deneddylation/derubylation activity (PubMed:15486099). Required for the
CC deneddylation of all cullins (PubMed:15923347, PubMed:17307927).
CC Essential for the structural integrity of the CSN holocomplex
CC (PubMed:17307927). {ECO:0000250, ECO:0000269|PubMed:11337587,
CC ECO:0000269|PubMed:15486099, ECO:0000269|PubMed:15923347,
CC ECO:0000269|PubMed:17307927, ECO:0000269|PubMed:9811788}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1, CSN2,
CC CSN3, CSN4, CSN5 (CSN5A or CSN5B), CSN6 (CSN6A or CSN6B), CSN7 and CSN8
CC (PubMed:9811788, PubMed:12615944, PubMed:15486099). CSN5A or CSN5B are
CC present within distinct CSN complexes each containing only one copy of
CC CSN5 (PubMed:15486099). Interacts with itself (PubMed:9811788). In the
CC complex, it is located in the center and probably interacts directly
CC with CSN4 and CSN6A or CSN6B (PubMed:9811788, PubMed:12615944). Present
CC also in subcomplex forms which inculdes CSN3 (PubMed:15486099). Also
CC exists as monomeric form (PubMed:9811788). Interacts with CYT1 in
CC vitro, but not in planta (PubMed:23424245).
CC {ECO:0000269|PubMed:12615944, ECO:0000269|PubMed:15486099,
CC ECO:0000269|PubMed:23424245, ECO:0000269|PubMed:9811788}.
CC -!- INTERACTION:
CC Q8LAZ7; P45432: CSN1; NbExp=3; IntAct=EBI-531132, EBI-530996;
CC Q8LAZ7; Q8W206: CSN6A; NbExp=3; IntAct=EBI-531132, EBI-531094;
CC Q8LAZ7; Q1EC57; NbExp=2; IntAct=EBI-531132, EBI-4481871;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9811788}. Nucleus
CC {ECO:0000269|PubMed:9811788}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LAZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LAZ7-2; Sequence=VSP_058794;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in flowers
CC and roots. Expressed at lower level in seedlings and siliques.
CC {ECO:0000269|PubMed:9811788}.
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 -!- DISRUPTION PHENOTYPE: Short hypocotyl and open cotyledons in dark-grown
CC seedling, accumulation of anthocyanin and expression of light-induced
CC genes in the dark resulting from an impaired cullin deneddylation
CC (PubMed:15923347). Severe developmental defects resulting in dwarf
CC stature and loss of apical dominance (PubMed:17307927). Csn5a and csn5b
CC double mutants are lethal at the seedling stage (PubMed:17307927).
CC {ECO:0000269|PubMed:15923347, ECO:0000269|PubMed:17307927}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF087413; AAC36344.1; -; mRNA.
DR EMBL; AF395062; AAL58105.1; -; mRNA.
DR EMBL; AF042334; AAB96974.1; -; mRNA.
DR EMBL; AF000657; AAB72159.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30309.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30310.1; -; Genomic_DNA.
DR EMBL; BT029486; ABL66743.1; -; mRNA.
DR EMBL; AY087510; AAM65053.1; -; mRNA.
DR EMBL; BT003909; AAO41956.1; -; mRNA.
DR PIR; C86363; C86363.
DR PIR; T52180; T52180.
DR RefSeq; NP_173705.1; NM_102139.2. [Q8LAZ7-1]
DR RefSeq; NP_973890.1; NM_202161.1. [Q8LAZ7-2]
DR AlphaFoldDB; Q8LAZ7; -.
DR SMR; Q8LAZ7; -.
DR BioGRID; 24138; 154.
DR IntAct; Q8LAZ7; 153.
DR STRING; 3702.AT1G22920.1; -.
DR MEROPS; M67.A01; -.
DR iPTMnet; Q8LAZ7; -.
DR MetOSite; Q8LAZ7; -.
DR PaxDb; Q8LAZ7; -.
DR PRIDE; Q8LAZ7; -.
DR ProteomicsDB; 222623; -. [Q8LAZ7-1]
DR EnsemblPlants; AT1G22920.1; AT1G22920.1; AT1G22920. [Q8LAZ7-1]
DR EnsemblPlants; AT1G22920.2; AT1G22920.2; AT1G22920. [Q8LAZ7-2]
DR GeneID; 838899; -.
DR Gramene; AT1G22920.1; AT1G22920.1; AT1G22920. [Q8LAZ7-1]
DR Gramene; AT1G22920.2; AT1G22920.2; AT1G22920. [Q8LAZ7-2]
DR KEGG; ath:AT1G22920; -.
DR Araport; AT1G22920; -.
DR TAIR; locus:2017764; AT1G22920.
DR eggNOG; KOG1554; Eukaryota.
DR InParanoid; Q8LAZ7; -.
DR OMA; AYEYMSV; -.
DR PhylomeDB; Q8LAZ7; -.
DR PRO; PR:Q8LAZ7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LAZ7; baseline and differential.
DR Genevisible; Q8LAZ7; AT.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
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:0010387; P:COP9 signalosome assembly; IMP:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IGI:TAIR.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0000338; P:protein deneddylation; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IGI:TAIR.
DR GO; GO:0010093; P:specification of floral organ identity; IMP:TAIR.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF33; PTHR10410:SF33; 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 Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Hydrolase; Metal-binding; Metalloprotease; Nucleus;
KW Phytochrome signaling pathway; Protease; Reference proteome; Signalosome;
KW Zinc.
FT CHAIN 1..357
FT /note="COP9 signalosome complex subunit 5a"
FT /id="PRO_0000194844"
FT DOMAIN 59..196
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..155
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 330..357
FT /note="IKDILFNSARQSKKSADDSSDPEPMITS -> SKYNLTMLILFPLAVNGSMK
FT LT (in isoform 2)"
FT /id="VSP_058794"
FT MUTAGEN 142
FT /note="H->A: No effect on CSN complex integrity but
FT impaired CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 144
FT /note="H->A: No effect on CSN complex integrity but
FT impaired CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 149
FT /note="C->A: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 149
FT /note="C->S: No effect on CSN complex integrity but
FT impaired CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 155
FT /note="D->N: No effect on CSN complex integrity but
FT impaired CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 175
FT /note="D->E,N: No effect on CSN complex integrity but
FT impaired CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT CONFLICT 21
FT /note="P -> R (in Ref. 7; AAM65053)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="W -> G (in Ref. 1; AAC36344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 39731 MW; 08FAC28547FDEEFB CRC64;
MEGSSSAIAR KTWELENNIL PVEPTDSASD SIFHYDDASQ AKIQQEKPWA SDPNYFKRVH
ISALALLKMV VHARSGGTIE IMGLMQGKTE GDTIIVMDAF ALPVEGTETR VNAQSDAYEY
MVEYSQTSKL AGRLENVVGW YHSHPGYGCW LSGIDVSTQM LNQQYQEPFL AVVIDPTRTV
SAGKVEIGAF RTYPEGHKIS DDHVSEYQTI PLNKIEDFGV HCKQYYSLDI TYFKSSLDSH
LLDLLWNKYW VNTLSSSPLL GNGDYVAGQI SDLAEKLEQA ESQLANSRYG GIAPAGHQRR
KEDEPQLAKI TRDSAKITVE QVHGLMSQVI KDILFNSARQ SKKSADDSSD PEPMITS
