CP20C_ARATH
ID CP20C_ARATH Reviewed; 260 AA.
AC P34791; Q8LBZ9; Q9FPH5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic;
DE Short=PPIase CYP20-3;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 20 kDa 3;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase CYP20-3;
DE AltName: Full=Rotamase cyclophilin-4;
DE Flags: Precursor;
GN Name=CYP20-3; Synonyms=ROC4; OrderedLocusNames=At3g62030;
GN ORFNames=F21F14.200;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8132503; DOI=10.1016/s0021-9258(17)37130-2;
RA Lippuner V., Chou I.T., Scott S.V., Ettinger W.F., Theg S.M., Gasser C.S.;
RT "Cloning and characterization of chloroplast and cytosolic forms of
RT cyclophilin from Arabidopsis thaliana.";
RL J. Biol. Chem. 269:7863-7868(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9426607; DOI=10.1023/a:1005930024796;
RA Chou I.T., Gasser C.S.;
RT "Characterization of the cyclophilin gene family of Arabidopsis thaliana
RT and phylogenetic analysis of known cyclophilin proteins.";
RL Plant Mol. Biol. 35:873-892(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [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 PROTEIN SEQUENCE OF 117-125; 131-137; 183-192 AND 242-257, ACTIVITY
RP REGULATION, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-131; CYS-206; CYS-248
RP AND CYS-253.
RX PubMed=12923164; DOI=10.1074/jbc.m304258200;
RA Motohashi K., Koyama F., Nakanishi Y., Ueoka-Nakanishi H., Hisabori T.;
RT "Chloroplast cyclophilin is a target protein of thioredoxin. Thiol
RT modulation of the peptidyl-prolyl cis-trans isomerase activity.";
RL J. Biol. Chem. 278:31848-31852(2003).
RN [8]
RP PROTEIN SEQUENCE OF 80-94, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [9]
RP INTERACTION WITH AGROBACTERIUM VIRD2.
RX PubMed=9618535; DOI=10.1073/pnas.95.12.7040;
RA Deng W., Chen L., Wood D.W., Metcalfe T., Liang X., Gordon M.P., Comai L.,
RA Nester E.W.;
RT "Agrobacterium VirD2 protein interacts with plant host cyclophilins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7040-7045(1998).
RN [10]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [11]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15051864; DOI=10.1104/pp.103.022160;
RA Romano P.G.N., Horton P., Gray J.E.;
RT "The Arabidopsis cyclophilin gene family.";
RL Plant Physiol. 134:1268-1282(2004).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SAT1.
RC STRAIN=cv. Columbia;
RX PubMed=18845687; DOI=10.1073/pnas.0808204105;
RA Dominguez-Solis J.R., He Z., Lima A., Ting J., Buchanan B.B., Luan S.;
RT "A cyclophilin links redox and light signals to cysteine biosynthesis and
RT stress responses in chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16386-16391(2008).
RN [13]
RP FUNCTION.
RX PubMed=23671085; DOI=10.1073/pnas.1218872110;
RA Park S.W., Li W., Viehhauser A., He B., Kim S., Nilsson A.K.,
RA Andersson M.X., Kittle J.D., Ambavaram M.M., Luan S., Esker A.R., Tholl D.,
RA Cimini D., Ellerstrom M., Coaker G., Mitchell T.K., Pereira A., Dietz K.J.,
RA Lawrence C.B.;
RT "Cyclophilin 20-3 relays a 12-oxo-phytodienoic acid signal during stress
RT responsive regulation of cellular redox homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9559-9564(2013).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Required for the light-induced increase of thiol
CC accumulation. Assists the folding or assembly of SAT1 enzyme to form
CC the cysteine synthase complex. Links light and redox signals to the
CC regulation of cysteine biosynthesis in response to stress.
CC {ECO:0000269|PubMed:18845687, ECO:0000269|PubMed:23671085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase. PPIase activity is
CC optimal in reduced form and minimal in oxidized form. Reduction of the
CC oxidized form is mediated by thioredoxin (TRX-M).
CC {ECO:0000269|PubMed:12923164}.
CC -!- SUBUNIT: Interacts with SAT1 and A.tumefaciens VirD2.
CC {ECO:0000269|PubMed:18845687, ECO:0000269|PubMed:9618535}.
CC -!- INTERACTION:
CC P34791; Q9SV07: ASAT1; NbExp=3; IntAct=EBI-449385, EBI-2025397;
CC P34791; Q42588: SAT1; NbExp=3; IntAct=EBI-449385, EBI-1633480;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:8132503}.
CC Note=Probably associated to membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P34791-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly expressed in leaves and flowers.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:8132503}.
CC -!- INDUCTION: Strongly induced by light. {ECO:0000269|PubMed:9426607}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to high light and rose bengal.
CC {ECO:0000269|PubMed:18845687}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; L14845; AAA20048.1; -; mRNA.
DR EMBL; U42724; AAB96831.1; -; Genomic_DNA.
DR EMBL; AL138642; CAB71910.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80297.1; -; Genomic_DNA.
DR EMBL; AF325026; AAG40378.1; -; mRNA.
DR EMBL; AY059843; AAL24325.1; -; mRNA.
DR EMBL; AY093284; AAM13283.1; -; mRNA.
DR EMBL; AY086899; AAM63944.1; -; mRNA.
DR PIR; B53422; B53422.
DR RefSeq; NP_191762.1; NM_116068.5. [P34791-1]
DR AlphaFoldDB; P34791; -.
DR SMR; P34791; -.
DR BioGRID; 10690; 7.
DR DIP; DIP-32746N; -.
DR IntAct; P34791; 4.
DR STRING; 3702.AT3G62030.2; -.
DR MetOSite; P34791; -.
DR SWISS-2DPAGE; P34791; -.
DR PaxDb; P34791; -.
DR PRIDE; P34791; -.
DR EnsemblPlants; AT3G62030.1; AT3G62030.1; AT3G62030. [P34791-1]
DR GeneID; 825376; -.
DR Gramene; AT3G62030.1; AT3G62030.1; AT3G62030. [P34791-1]
DR KEGG; ath:AT3G62030; -.
DR Araport; AT3G62030; -.
DR eggNOG; KOG0880; Eukaryota.
DR InParanoid; P34791; -.
DR PhylomeDB; P34791; -.
DR BRENDA; 5.2.1.8; 399.
DR PRO; PR:P34791; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P34791; baseline and differential.
DR Genevisible; P34791; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Chloroplast; Direct protein sequencing;
KW Disulfide bond; Isomerase; Plastid; Reference proteome; Rotamase;
KW Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 80..260
FT /note="Peptidyl-prolyl cis-trans isomerase CYP20-3,
FT chloroplastic"
FT /id="PRO_0000025476"
FT DOMAIN 98..255
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT DISULFID 131..248
FT /evidence="ECO:0000269|PubMed:12923164"
FT DISULFID 206..253
FT /evidence="ECO:0000269|PubMed:12923164"
FT MUTAGEN 131
FT /note="C->S: Reduced PPIase activity, lower sensitivity to
FT redox regulation; when associated with S-248."
FT /evidence="ECO:0000269|PubMed:12923164"
FT MUTAGEN 206
FT /note="C->S: Reduced PPIase activity, lower sensitivity to
FT redox regulation; when associated with S-253."
FT /evidence="ECO:0000269|PubMed:12923164"
FT MUTAGEN 248
FT /note="C->S: Reduced PPIase activity, lower sensitivity to
FT redox regulation; when associated with S-131."
FT /evidence="ECO:0000269|PubMed:12923164"
FT MUTAGEN 253
FT /note="C->S: Reduced PPIase activity, lower sensitivity to
FT redox regulation; when associated with S-206."
FT /evidence="ECO:0000269|PubMed:12923164"
FT CONFLICT 87
FT /note="I -> T (in Ref. 6; AAM63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Q -> K (in Ref. 5; AAG40378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 28208 MW; D412AECBB8A5A3B7 CRC64;
MASSSSMQMV HTSRSIAQIG FGVKSQLVSA NRTTQSVCFG ARSSGIALSS RLHYASPIKQ
FSGVYATTKH QRTACVKSMA AEEEEVIEPQ AKVTNKVYFD VEIGGEVAGR IVMGLFGEVV
PKTVENFRAL CTGEKKYGYK GSSFHRIIKD FMIQGGDFTE GNGTGGISIY GAKFEDENFT
LKHTGPGILS MANAGPNTNG SQFFICTVKT SWLDNKHVVF GQVIEGMKLV RTLESQETRA
FDVPKKGCRI YACGELPLDA
