MPSR1_ARATH
ID MPSR1_ARATH Reviewed; 204 AA.
AC Q9LQX2; Q8LCT4;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=E3 ubiquitin-protein ligase MPSR1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:29087340};
DE AltName: Full=Protein MISFOLDED PROTEIN SENSING RING E3 LIGASE 1 {ECO:0000303|PubMed:29087340};
DE AltName: Full=RING-type E3 ubiquitin transferase MPSR1 {ECO:0000305};
GN Name=MPSR1 {ECO:0000303|PubMed:29087340};
GN OrderedLocusNames=At1g26800 {ECO:0000312|Araport:AT1G26800};
GN ORFNames=T24P13.19 {ECO:0000312|EMBL:AAF87040.1};
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].
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP AUTOUBIQUITINATION.
RX PubMed=29087340; DOI=10.1073/pnas.1713574114;
RA Kim J.H., Cho S.K., Oh T.R., Ryu M.Y., Yang S.W., Kim W.T.;
RT "MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded
RT proteins in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E10009-E10017(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in protein quality
CC control (PQC) under proteotoxic stress. Is essential to plant survival
CC under proteotoxic stress. Functions by removing damaged proteins before
CC they form cytotoxic aggregates. Recognizes misfolded proteins
CC selectively and tethers polyubiquitin chains to the proteins directly
CC for subsequent degradation by the 26S proteasome pathway. Targets
CC misfolded proteins independently of cytoplasmic chaperones. Associates
CC with the 26S proteasome and sustains the structural integrity of the
CC proteasome complex at the initial stage of proteotoxic stress. Under
CC normal conditions, MPSR1 becomes highly unstable by its
CC autoubiquitination activity and is stabilized during proteotoxic stress
CC by conjugating ubiquitins on misfolded proteins.
CC {ECO:0000269|PubMed:29087340}.
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:29087340};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29087340}.
CC -!- INDUCTION: Induced by arsenite and the proline toxic analog azetidine-
CC 2-carboxylate. {ECO:0000269|PubMed:29087340}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:29087340}.
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DR EMBL; AC006535; AAF87040.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30743.1; -; Genomic_DNA.
DR EMBL; AF361638; AAK32806.1; -; mRNA.
DR EMBL; AY052705; AAK96609.1; -; mRNA.
DR EMBL; AY055097; AAL05897.1; -; mRNA.
DR EMBL; AY086415; AAM63417.1; -; mRNA.
DR RefSeq; NP_564263.1; NM_102444.3.
DR AlphaFoldDB; Q9LQX2; -.
DR SMR; Q9LQX2; -.
DR IntAct; Q9LQX2; 1.
DR STRING; 3702.AT1G26800.1; -.
DR PaxDb; Q9LQX2; -.
DR PRIDE; Q9LQX2; -.
DR EnsemblPlants; AT1G26800.1; AT1G26800.1; AT1G26800.
DR GeneID; 839223; -.
DR Gramene; AT1G26800.1; AT1G26800.1; AT1G26800.
DR KEGG; ath:AT1G26800; -.
DR Araport; AT1G26800; -.
DR TAIR; locus:2200610; AT1G26800.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_091490_0_0_1; -.
DR InParanoid; Q9LQX2; -.
DR OMA; YNMPVDE; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q9LQX2; -.
DR PRO; PR:Q9LQX2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQX2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051787; F:misfolded protein binding; IDA:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0071218; P:cellular response to misfolded protein; IDA:TAIR.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0061635; P:regulation of protein complex stability; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Stress response; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..204
FT /note="E3 ubiquitin-protein ligase MPSR1"
FT /id="PRO_0000442932"
FT ZN_FING 113..154
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 6
FT /note="E -> D (in Ref. 4; AAM63417)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="S -> P (in Ref. 4; AAM63417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 22735 MW; 5E2357E8EEEDEEFA CRC64;
MATEQEAEVG TETSSVSGRF LRNRDLYLFL PFLLGFSDQE SSNGDDDDVA SSRERIILVN
PFTQGMIVLE GSSGMNPLLR SLLESREEGR PPASKASIDA MPIVEIDGCE GECVICLEEW
KSEETVKEMP CKHRFHGGCI EKWLGFHGSC PVCRYEMPVD GDEIGKKRND GNEIWVRFSF
NDGRRIRDFS AQDGGNSDGV ESEN
