CSU1_ARATH
ID CSU1_ARATH Reviewed; 310 AA.
AC Q9SY88; Q8GZ68;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase CSU1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:24838976};
DE AltName: Full=Protein COP1 SUPPRESSOR 1 {ECO:0000303|PubMed:24838976};
DE AltName: Full=RING-type E3 ubiquitin transferase CSU1 {ECO:0000305};
GN Name=CSU1 {ECO:0000303|PubMed:24838976};
GN OrderedLocusNames=At1g61620 {ECO:0000312|Araport:AT1G61620};
GN ORFNames=T25B24.3 {ECO:0000312|EMBL:AAD25548.1};
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].
RC TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=24838976; DOI=10.1105/tpc.114.124024;
RA Xu D., Lin F., Jiang Y., Huang X., Li J., Ling J., Hettiarachchi C.,
RA Tellgren-Roth C., Holm M., Deng X.W.;
RT "The RING-finger E3 ubiquitin ligase COP1 SUPPRESSOR1 negatively regulates
RT COP1 abundance in maintaining COP1 homeostasis in dark-grown Arabidopsis
RT seedlings.";
RL Plant Cell 26:1981-1991(2014).
CC -!- FUNCTION: RING-finger E3 ubiquitin-protein ligase that plays an major
CC role in maintaining COP1 homeostasis in darkness. Negatively regulates
CC COP1 protein accumulation by targeting COP1 for ubiquitination and
CC subsequent proteasomal degradation in dark-grown seedlings. Negatively
CC regulates the accumulation of SPA1 protein in the dark.
CC {ECO:0000269|PubMed:24838976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:24838976};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24838976}. Nucleus
CC speckle {ECO:0000269|PubMed:24838976}. Note=Is recruited to nuclear
CC speckles by COP1 in the dark. {ECO:0000269|PubMed:24838976}.
CC -!- SIMILARITY: Belongs to the NOSIP family. {ECO:0000305}.
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DR EMBL; DQ059102; AAY57588.1; -; mRNA.
DR EMBL; AC005850; AAD25548.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33863.1; -; Genomic_DNA.
DR EMBL; AK117181; BAC41858.1; -; mRNA.
DR EMBL; BT026113; ABG48469.1; -; mRNA.
DR EMBL; AY085557; AAM62779.1; -; mRNA.
DR PIR; F96641; F96641.
DR RefSeq; NP_564781.1; NM_104844.3.
DR AlphaFoldDB; Q9SY88; -.
DR IntAct; Q9SY88; 1.
DR STRING; 3702.AT1G61620.1; -.
DR PaxDb; Q9SY88; -.
DR PRIDE; Q9SY88; -.
DR ProteomicsDB; 222721; -.
DR EnsemblPlants; AT1G61620.1; AT1G61620.1; AT1G61620.
DR GeneID; 842458; -.
DR Gramene; AT1G61620.1; AT1G61620.1; AT1G61620.
DR KEGG; ath:AT1G61620; -.
DR Araport; AT1G61620; -.
DR TAIR; locus:2200898; AT1G61620.
DR eggNOG; KOG3039; Eukaryota.
DR HOGENOM; CLU_053742_1_0_1; -.
DR InParanoid; Q9SY88; -.
DR OMA; AKEKRPM; -.
DR OrthoDB; 1567031at2759; -.
DR PhylomeDB; Q9SY88; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SY88; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY88; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IGI:TAIR.
DR GO; GO:0031648; P:protein destabilization; IEP:TAIR.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR016818; NOSIP.
DR InterPro; IPR031790; Znf-NOSIP.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13063; PTHR13063; 1.
DR Pfam; PF15906; zf-NOSIP; 1.
DR PIRSF; PIRSF023577; ENOS_interacting; 1.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..310
FT /note="E3 ubiquitin-protein ligase CSU1"
FT /id="PRO_0000441873"
FT ZN_FING 43..67
FT /note="RING-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 221..263
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 110..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..95
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="I -> M (in Ref. 4; BAC41858)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="N -> D (in Ref. 4; BAC41858)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="G -> V (in Ref. 4; BAC41858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 35024 MW; 0051B9BF6D4CD00F CRC64;
MPQRHSKNNN DLAYFTYDEK KKLGYGTQRE RLGRDSIKPF DACSLCLKPF IDPMCCHKGH
VFCRECILEC FLAQKKDIQR RLAAHSSQKK QDKDEEEERL MLQKARELDE FDQQNHSAMP
RNSDKNHNED KNGFHGANSV KTTSFEEEAL RTMKAFWLPS ATPAASVRVD APETHTVCPE
GKEKLKLKNL FAIRFTEDNS EEEETKTKSA SSSSYDKSYI CPSCKVTLTN TMSLVALSSC
GHVFCKKCAE KFMPVDKVCL VCDKPCKDRN LVGLKKGGTG FAEHDDHLEA KEYKHLGSGS
GLGLVRPVKT
