CSU2_ARATH
ID CSU2_ARATH Reviewed; 279 AA.
AC F4HVZ5; Q94JU5; Q9FZ28;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein COP1 SUPPRESSOR 2 {ECO:0000303|PubMed:26714275};
GN Name=CSU2 {ECO:0000303|PubMed:26714275};
GN OrderedLocusNames=At1g02330 {ECO:0000312|Araport:AT1G02330};
GN ORFNames=T6A9.2 {ECO:0000312|EMBL:AEE27416.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-279.
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 [4]
RP FUNCTION, INTERACTION WITH COP1, AND SUBCELLULAR LOCATION.
RX PubMed=26714275; DOI=10.1371/journal.pgen.1005747;
RA Xu D., Lin F., Jiang Y., Ling J., Hettiarachchi C., Tellgren-Roth C.,
RA Holm M., Wei N., Deng X.W.;
RT "Arabidopsis COP1 SUPPRESSOR 2 represses COP1 E3 ubiquitin ligase activity
RT through their coiled-coil domains association.";
RL PLoS Genet. 11:E1005747-E1005747(2015).
CC -!- FUNCTION: Inhibits E3 ubiquitin-protein ligase activity of COP1, a
CC central repressor of seedling photomorphogenesis. Represses COP1-
CC mediated turnover of HY5 in the dark. Required for primary root
CC development under normal light growth conditions.
CC {ECO:0000269|PubMed:26714275}.
CC -!- SUBUNIT: Interacts with COP1. {ECO:0000269|PubMed:26714275}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26714275}. Nucleus
CC speckle {ECO:0000269|PubMed:26714275}. Note=Is recruited to nuclear
CC speckles by COP1. {ECO:0000269|PubMed:26714275}.
CC -!- SIMILARITY: Belongs to the TLS1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00884.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC064879; AAG00884.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27416.1; -; Genomic_DNA.
DR EMBL; AF372932; AAK50072.1; -; mRNA.
DR EMBL; AY133621; AAM91451.1; -; mRNA.
DR PIR; E86153; E86153.
DR RefSeq; NP_563649.1; NM_100114.5.
DR AlphaFoldDB; F4HVZ5; -.
DR SMR; F4HVZ5; -.
DR STRING; 3702.AT1G02330.1; -.
DR iPTMnet; F4HVZ5; -.
DR PaxDb; F4HVZ5; -.
DR PRIDE; F4HVZ5; -.
DR ProteomicsDB; 222696; -.
DR EnsemblPlants; AT1G02330.1; AT1G02330.1; AT1G02330.
DR GeneID; 839367; -.
DR Gramene; AT1G02330.1; AT1G02330.1; AT1G02330.
DR KEGG; ath:AT1G02330; -.
DR Araport; AT1G02330; -.
DR TAIR; locus:2204888; AT1G02330.
DR eggNOG; KOG3345; Eukaryota.
DR HOGENOM; CLU_068345_0_0_1; -.
DR InParanoid; F4HVZ5; -.
DR OMA; IHNIEAT; -.
DR OrthoDB; 1493869at2759; -.
DR PRO; PR:F4HVZ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HVZ5; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0010099; P:regulation of photomorphogenesis; IGI:TAIR.
DR GO; GO:0055121; P:response to high fluence blue light stimulus by blue high-fluence system; IMP:TAIR.
DR InterPro; IPR010756; Tls1.
DR PANTHER; PTHR13486; PTHR13486; 1.
DR Pfam; PF07052; Hep_59; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome.
FT CHAIN 1..279
FT /note="Protein COP1 SUPPRESSOR 2"
FT /id="PRO_0000441872"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..183
FT /evidence="ECO:0000305|PubMed:26714275"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 32349 MW; 0A7BBA1C3241029A CRC64;
MPPKRNFRKR SFEEEEEDND VNKAAISEEE EKRRLALEEV KFLQKLRERK LGIPALSSTA
QSSIGKVKPV EKTETEGEKE ELVLQDTFAQ ETAVLIEDPN MVKYIEQELA KKRGRNIDDA
EEVENELKRV EDELYKIPDH LKVKKRSSEE SSTQWTTGIA EVQLPIEYKL KNIEETEAAK
KLLQERRLMG RPKSEFSIPS SYSADYFQRG KDYAEKLRRE HPELYKDRGG PQADGEAAKP
STSSSTNNNA DSGKSRQAAT DQIMLERFRK RERNRVMRR
