CSN5_ORYSJ
ID CSN5_ORYSJ Reviewed; 360 AA.
AC Q8H936; Q7XTD8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=COP9 signalosome complex subunit 5 {ECO:0000303|PubMed:27137867};
DE Short=OsCSN5 {ECO:0000303|PubMed:27137867};
DE AltName: Full=JUN-activation-domain-binding protein 1 {ECO:0000312|EMBL:BAC22747.1};
DE AltName: Full=Signalosome subunit 6 {ECO:0000305};
GN Name=CSN5 {ECO:0000303|PubMed:27137867};
GN Synonyms=JAB1 {ECO:0000312|EMBL:BAC22747.1};
GN OrderedLocusNames=Os04g0654700 {ECO:0000312|EMBL:BAF16026.1};
GN ORFNames=OSJNBb0022F16.7 {ECO:0000312|EMBL:CAE01552.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RA Yamamoto T., Mori Y., Kimura S., Sakaguchi K.;
RT "Oryza sativa japonica group Jab1 gene for JUN-activation-domain-binding
RT protein 1.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP INTERACTION WITH MCM2.
RX PubMed=18755073; DOI=10.5483/bmbrep.2008.41.8.581;
RA Cho J.H., Kim H.B., Kim H.S., Choi S.B.;
RT "Identification and characterization of a rice MCM2 homologue required for
RT DNA replication.";
RL BMB Rep. 41:581-586(2008).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=27137867; DOI=10.1038/srep25485;
RA Tan S., Liu F., Pan X.X., Zang Y.P., Jin F., Zu W.X., Qi X.T., Xiao W.,
RA Yin L.P.;
RT "CSN6, a subunit of the COP9 signalosome, is involved in early response to
RT iron deficiency in Oryza sativa.";
RL Sci. Rep. 6:25485-25485(2016).
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 response to hormones (By
CC similarity). The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF (By similarity). Involved in early response to
CC iron deficiency (Probable). {ECO:0000250|UniProtKB:Q6ZKM2,
CC ECO:0000305|PubMed:27137867}.
CC -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1, CSN2,
CC CSN3, CSN4, CSN5, CSN6, CSN7 and CSN8 (By similarity). Interacts with
CC MCM2 (PubMed:18755073). {ECO:0000250|UniProtKB:Q8LAZ7,
CC ECO:0000269|PubMed:18755073}.
CC -!- INDUCTION: Down-regulated during the early stage of iron deficiency (at
CC protein level). {ECO:0000269|PubMed:27137867}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB095022; BAC22747.1; -; Genomic_DNA.
DR EMBL; AL606446; CAE01552.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF16026.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91398.1; -; Genomic_DNA.
DR PIR; T02934; T02934.
DR RefSeq; XP_015637190.1; XM_015781704.1.
DR AlphaFoldDB; Q8H936; -.
DR SMR; Q8H936; -.
DR STRING; 4530.OS04T0654700-02; -.
DR MEROPS; M67.A02; -.
DR PaxDb; Q8H936; -.
DR PRIDE; Q8H936; -.
DR EnsemblPlants; Os04t0654700-01; Os04t0654700-01; Os04g0654700.
DR EnsemblPlants; Os04t0654700-02; Os04t0654700-02; Os04g0654700.
DR GeneID; 4337249; -.
DR Gramene; Os04t0654700-01; Os04t0654700-01; Os04g0654700.
DR Gramene; Os04t0654700-02; Os04t0654700-02; Os04g0654700.
DR KEGG; osa:4337249; -.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; Q8H936; -.
DR OMA; ALWNKYW; -.
DR OrthoDB; 1031881at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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:0000338; P:protein deneddylation; IBA:GO_Central.
DR GO; GO:1990641; P:response to iron ion starvation; IDA:UniProtKB.
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 Developmental protein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signalosome; Zinc.
FT CHAIN 1..360
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000446887"
FT DOMAIN 60..197
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 293..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..156
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 360 AA; 40037 MW; 7A9F53270DD26A85 CRC64;
MEPTSSAAMA RQTWELENNI PAAASDPDAL DAIYRYDEAA QARVQQEKPW ANDPHPFRRA
KISALALLKM VVHARAGGTI EVMGLMQGKC EGDAIVVMDA FALPVEGTET RVNAQADAYE
YMVEYSTINK QAGRLENVVG WYHSHPGYGC WLSGIDVSTQ MLNQQFQEPF LAVVIDPTRT
VSAGKVEIGA FRTYPKDYKP PDEPVSEYQT IPLNKIEDFG VHCKQYYALD ITYFKSSLDS
HLLDLLWNKY WVNTLSSSPL LGNRDYVAGQ IFDLADKLEQ AEGQLAHSRY GMLMPSQRKK
EQEESPLAKV TRDSSKITAE QVHGLMSQVI KDILFNSVHP SNKASTSAPD SSGPEPMVEA
