P34790 (CP18C_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP18-3
Short name=PPIase CYP18-3
EC=5.2.1.8

Alternative name(s):
Cyclophilin of 18 kDa 3
Cyclosporin A-binding protein
Rotamase cyclophilin-1

Gene names

Name:	CYP18-3
Synonyms:	ROC1
Ordered Locus Names:	At4g38740
ORF Names:	T9A14.20

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Triggers the activation of bacterial AvrRpt2 protease activity upon infection by P.syringae. Activated AvrRpt2 confers virulence in plant lacking the RPS2 resistance gene. In plants expressing RPS2, the AvrRpt2-mediated degradation of RIN4 activates RPS2, which induces hypersensitive response (HR) and plant resistance. Ref.11
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subunit structure	Interacts with P.syringae AvrRpt2. Ref.11
Subcellular location	Cytoplasm Probable.
Tissue specificity	Pollen (at protein level). Ubiquitous. Ref.1 Ref.7 Ref.9 Ref.10
Induction	By light and by wounding. Ref.6
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	Hypersensitive response Plant defense
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Chaperone Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	plant-type hypersensitive response Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 172	172	Peptidyl-prolyl cis-trans isomerase CYP18-3		PRO_0000064133
Regions
	Domain	7 – 170	164	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P34790 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: B49B8C68E60E15E1	FASTA	172	18,373
	10 20 30 40 50 60 MAFPKVYFDM TIDGQPAGRI VMELYTDKTP RTAENFRALC TGEKGVGGTG KPLHFKGSKF 70 80 90 100 110 120 HRVIPNFMCQ GGDFTAGNGT GGESIYGSKF EDENFERKHT GPGILSMANA GANTNGSQFF 130 140 150 160 170 ICTVKTDWLD GKHVVFGQVV EGLDVVKAIE KVGSSSGKPT KPVVVADCGQ LS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana." Lippuner V., Chou I.T., Scott S.V., Ettinger W.F., Theg S.M., Gasser C.S. J. Biol. Chem. 269:7863-7868(1994) [PubMed: 8132503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins." Chou I.T., Gasser C.S. Plant Mol. Biol. 35:873-892(1997) [PubMed: 9426607] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia. Tissue: Leaf.
[7]	"Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis." He Z., Li L., Luan S. Plant Physiol. 134:1248-1267(2004) [PubMed: 15047905] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"The Arabidopsis cyclophilin gene family." Romano P.G.N., Horton P., Gray J.E. Plant Physiol. 134:1268-1282(2004) [PubMed: 15051864] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"A reference map of the Arabidopsis thaliana mature pollen proteome." Noir S., Braeutigam A., Colby T., Schmidt J., Panstruga R. Biochem. Biophys. Res. Commun. 337:1257-1266(2005) [PubMed: 16242667] [Abstract] Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"Proteome mapping of mature pollen of Arabidopsis thaliana." Holmes-Davis R., Tanaka C.K., Vensel W.H., Hurkman W.J., McCormick S. Proteomics 5:4864-4884(2005) [PubMed: 16247729] [Abstract] Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[11]	"Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin." Coaker G., Falick A., Staskawicz B.J. Science 308:548-550(2005) [PubMed: 15746386] [Abstract] Cited for: FUNCTION, INTERACTION WITH AVRRPT2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14844 mRNA. Translation: AAA20047.1. AL035656 Genomic DNA. Translation: CAB38608.1. AL161593 Genomic DNA. Translation: CAB80537.1. CP002687 Genomic DNA. Translation: AEE86970.1. AY093227 mRNA. Translation: AAM13226.1. BT003397 mRNA. Translation: AAO30060.1. AY088103 mRNA. Translation: AAM65649.1.
IPI	IPI00540225.
PIR	T06073.
RefSeq	NP_195585.1. NM_120034.2.
UniGene	At.24097. At.24759. At.71539. At.72496.
3D structure databases
ProteinModelPortal	P34790.
SMR	P34790. Positions 1-171.
ModBase	Search...
Protein-protein interaction databases
IntAct	P34790. 2 interactions.
STRING	P34790.
Proteomic databases
PRIDE	P34790.
ProMEX	P34790.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G38740.1; AT4G38740.1; AT4G38740.
GeneID	830029.
GenomeReviews	Gene locus AT4G38740 in contig CT486007_GR.
KEGG	ath:AT4G38740.
Organism-specific databases
TAIR	At4g38740.
Phylogenomic databases
eggNOG	KOG0865.
HOGENOM	HBG610621.
InParanoid	P34790.
OMA	YFDMTID.
PhylomeDB	P34790.
ProtClustDB	CLSN2683570.
Enzyme and pathway databases
BRENDA	5.2.1.8. 399.
Gene expression databases
ArrayExpress	P34790.
Genevestigator	P34790.
GermOnline	AT4G38740. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K01802.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP18C_ARATH

Accession

Primary (citable) accession number: P34790

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program