CP18C_ARATH
ID CP18C_ARATH Reviewed; 172 AA.
AC P34790; Q0WWG0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP18-3;
DE Short=PPIase CYP18-3;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 18 kDa 3;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase cyclophilin-1;
GN Name=CYP18-3; Synonyms=ROC1; OrderedLocusNames=At4g38740;
GN ORFNames=T9A14.20;
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], 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
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 INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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 [8]
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 [9]
RP TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND INDUCTION.
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 [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH AVRRPT2.
RX PubMed=15746386; DOI=10.1126/science.1108633;
RA Coaker G., Falick A., Staskawicz B.J.;
RT "Activation of a phytopathogenic bacterial effector protein by a eukaryotic
RT cyclophilin.";
RL Science 308:548-550(2005).
RN [12]
RP FUNCTION, MUTAGENESIS OF ARG-62; TRP-128 AND HIS-133, 3D-STRUCTURE
RP MODELING, AND INTERACTION WITH AVRRPT2.
RX PubMed=16968222; DOI=10.1111/j.1365-2958.2006.05335.x;
RA Coaker G., Zhu G., Ding Z., Van Doren S.R., Staskawicz B.;
RT "Eukaryotic cyclophilin as a molecular switch for effector activation.";
RL Mol. Microbiol. 61:1485-1496(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH AVRRPT2.
RX PubMed=20050698; DOI=10.1021/bi901813e;
RA Aumueller T., Jahreis G., Fischer G., Schiene-Fischer C.;
RT "Role of prolyl cis/trans isomers in cyclophilin-assisted Pseudomonas
RT syringae AvrRpt2 protease activation.";
RL Biochemistry 49:1042-1052(2010).
RN [14]
RP FUNCTION, INDUCTION BY LIGHT, AND LACK OF INTERACTION WITH BES1.
RX PubMed=22463079; DOI=10.1111/j.1365-313x.2012.05013.x;
RA Trupkin S.A., Mora-Garcia S., Casal J.J.;
RT "The cyclophilin ROC1 links phytochrome and cryptochrome to brassinosteroid
RT sensitivity.";
RL Plant J. 71:712-723(2012).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Involved in de-etiolation. Reduces the sensitivity to
CC brassinosteroids by decreasing somehow the abundance of the partially
CC dephosphorylated form of BES1. Triggers the activation of bacterial
CC AvrRpt2 protease activity upon infection by P.syringae. Activated
CC AvrRpt2 confers virulence in plant lacking the RPS2 resistance gene. In
CC plants expressing RPS2, the AvrRpt2-mediated degradation of RIN4
CC activates RPS2, which induces hypersensitive response (HR) and plant
CC resistance. {ECO:0000269|PubMed:15746386, ECO:0000269|PubMed:16968222,
CC ECO:0000269|PubMed:20050698, ECO:0000269|PubMed:22463079}.
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.
CC -!- SUBUNIT: Interacts with P.syringae AvrRpt2 and with A.tumefaciens
CC VirD2, but not with BES1. {ECO:0000269|PubMed:15746386,
CC ECO:0000269|PubMed:16968222, ECO:0000269|PubMed:20050698,
CC ECO:0000269|PubMed:9618535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:8132503}.
CC -!- INDUCTION: Up-regulated by light, salt and wounding. Down-regulated by
CC cytokinin treatment. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:22463079, ECO:0000269|PubMed:9426607}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L14844; AAA20047.1; -; mRNA.
DR EMBL; AL035656; CAB38608.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80537.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86970.1; -; Genomic_DNA.
DR EMBL; AY093227; AAM13226.1; -; mRNA.
DR EMBL; BT003397; AAO30060.1; -; mRNA.
DR EMBL; AK226392; BAE98538.1; -; mRNA.
DR EMBL; AY088103; AAM65649.1; -; mRNA.
DR PIR; T06073; T06073.
DR RefSeq; NP_195585.1; NM_120034.2.
DR AlphaFoldDB; P34790; -.
DR SMR; P34790; -.
DR BioGRID; 15309; 6.
DR IntAct; P34790; 2.
DR STRING; 3702.AT4G38740.1; -.
DR iPTMnet; P34790; -.
DR MetOSite; P34790; -.
DR PaxDb; P34790; -.
DR PRIDE; P34790; -.
DR ProteomicsDB; 240659; -.
DR EnsemblPlants; AT4G38740.1; AT4G38740.1; AT4G38740.
DR GeneID; 830029; -.
DR Gramene; AT4G38740.1; AT4G38740.1; AT4G38740.
DR KEGG; ath:AT4G38740; -.
DR Araport; AT4G38740; -.
DR TAIR; locus:2141747; AT4G38740.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P34790; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P34790; -.
DR BRENDA; 5.2.1.8; 399.
DR PRO; PR:P34790; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P34790; baseline and differential.
DR Genevisible; P34790; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
DR GO; GO:0009785; P:blue light signaling pathway; IGI:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0009704; P:de-etiolation; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0009585; P:red, far-red light phototransduction; IGI:TAIR.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0007165; P:signal transduction; ISS:TAIR.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 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 Chaperone; Cytoplasm; Hypersensitive response; Isomerase; Plant defense;
KW Reference proteome; Rotamase.
FT CHAIN 1..172
FT /note="Peptidyl-prolyl cis-trans isomerase CYP18-3"
FT /id="PRO_0000064133"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MUTAGEN 62
FT /note="R->A: Loss of PPIase activity."
FT /evidence="ECO:0000269|PubMed:16968222"
FT MUTAGEN 128
FT /note="W->A: Loss of PPIase activity."
FT /evidence="ECO:0000269|PubMed:16968222"
FT MUTAGEN 133
FT /note="H->A: Decreased PPIase activity."
FT /evidence="ECO:0000269|PubMed:16968222"
SQ SEQUENCE 172 AA; 18373 MW; B49B8C68E60E15E1 CRC64;
MAFPKVYFDM TIDGQPAGRI VMELYTDKTP RTAENFRALC TGEKGVGGTG KPLHFKGSKF
HRVIPNFMCQ GGDFTAGNGT GGESIYGSKF EDENFERKHT GPGILSMANA GANTNGSQFF
ICTVKTDWLD GKHVVFGQVV EGLDVVKAIE KVGSSSGKPT KPVVVADCGQ LS
