P34791 (CP20C_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic
Short name=PPIase CYP20-3
EC=5.2.1.8

Alternative name(s):
Cyclophilin of 20 kDa 3
Cyclosporin A-binding protein
Rotamase CYP20-3
Rotamase cyclophilin-4

Gene names

Name:	CYP20-3
Synonyms:	ROC4
Ordered Locus Names:	At3g62030
ORF Names:	F21F14.200

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	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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. PPIase activity is optimal in reduced form and minimal in oxidized form. Reduction of the oxidized form is mediated by thioredoxin (TRX-M). Ref.7
Subcellular location	Plastid › chloroplast stroma. Note: Probably associated to membranes. Ref.1 Ref.8 Ref.9 Ref.10
Tissue specificity	Ubiquitous, mostly expressed in leaves and flowers. Ref.1 Ref.11
Induction	Strongly induced by light. Ref.2 Ref.7
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Cyclosporin
Molecular function	Chaperone Isomerase Rotamase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from mutant phenotype. Source: TAIR defense response to bacterium Inferred from expression pattern. Source: TAIR protein folding Inferred from electronic annotation. Source: UniProtKB-KW response to abscisic acid stimulus Inferred from expression pattern. Source: TAIR response to light intensity Inferred from mutant phenotype. Source: TAIR response to mannitol stimulus Inferred from mutant phenotype. Source: TAIR response to oxidative stress Inferred from mutant phenotype. Source: TAIR response to salt stress Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay Ref.9. Source: TAIR chloroplast stroma Inferred from direct assay Ref.1. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay Ref.10. Source: TAIR cytosolic ribosome Inferred from direct assay. Source: TAIR thylakoid lumen Inferred from direct assay Ref.8. Source: TAIR
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.1. Source: TAIR protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASAT1	Q9SV07	3	EBI-449385,EBI-2025397

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P34791-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 78	78	Chloroplast Potential
	Chain	79 – 260	182	Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic		PRO_0000025476
Regions
	Domain	98 – 255	158	PPIase cyclophilin-type
Amino acid modifications
	Disulfide bond	131 ↔ 248		Ref.7
	Disulfide bond	206 ↔ 253		Ref.7
Experimental info
	Mutagenesis	131	1	C → S: Reduced PPIase activity, lower sensitivity to redox regulation; when associated with S-248. Ref.7
	Mutagenesis	206	1	C → S: Reduced PPIase activity, lower sensitivity to redox regulation; when associated with S-253. Ref.7
	Mutagenesis	248	1	C → S: Reduced PPIase activity, lower sensitivity to redox regulation; when associated with S-131. Ref.7
	Mutagenesis	253	1	C → S: Reduced PPIase activity, lower sensitivity to redox regulation; when associated with S-206. Ref.7
	Sequence conflict	87	1	I → T in AAM63944. Ref.6
	Sequence conflict	202	1	Q → K in AAG40378. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: D412AECBB8A5A3B7	FASTA	260	28,208
	10 20 30 40 50 60 MASSSSMQMV HTSRSIAQIG FGVKSQLVSA NRTTQSVCFG ARSSGIALSS RLHYASPIKQ 70 80 90 100 110 120 FSGVYATTKH QRTACVKSMA AEEEEVIEPQ AKVTNKVYFD VEIGGEVAGR IVMGLFGEVV 130 140 150 160 170 180 PKTVENFRAL CTGEKKYGYK GSSFHRIIKD FMIQGGDFTE GNGTGGISIY GAKFEDENFT 190 200 210 220 230 240 LKHTGPGILS MANAGPNTNG SQFFICTVKT SWLDNKHVVF GQVIEGMKLV RTLESQETRA 250 260 FDVPKKGCRI YACGELPLDA

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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Leaf.
[2]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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.
[6]	"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].
[7]	"Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity." Motohashi K., Koyama F., Nakanishi Y., Ueoka-Nakanishi H., Hisabori T. J. Biol. Chem. 278:31848-31852(2003) [PubMed: 12923164] [Abstract] Cited for: PROTEIN SEQUENCE OF 117-125; 131-137; 183-192 AND 242-257, ENZYME REGULATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-131; CYS-206; CYS-248 AND CYS-253.
[8]	"Proteome map of the chloroplast lumen of Arabidopsis thaliana." Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P., Kieselbach T. J. Biol. Chem. 277:8354-8365(2002) [PubMed: 11719511] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis." Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S. J. Proteome Res. 2:413-425(2003) [PubMed: 12938931] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy." Peltier J.-B., Ytterberg A.J., Sun Q., van Wijk K.J. J. Biol. Chem. 279:49367-49383(2004) [PubMed: 15322131] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]	"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.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14845 mRNA. Translation: AAA20048.1. U42724 Genomic DNA. Translation: AAB96831.1. AL138642 Genomic DNA. Translation: CAB71910.1. CP002686 Genomic DNA. Translation: AEE80297.1. AF325026 mRNA. Translation: AAG40378.1. AY059843 mRNA. Translation: AAL24325.1. AY093284 mRNA. Translation: AAM13283.1. AY086899 mRNA. Translation: AAM63944.1.
IPI	IPI00517879.
PIR	B53422.
RefSeq	NP_191762.1. NM_116068.4.
UniGene	At.24742. At.48797.
3D structure databases
ProteinModelPortal	P34791.
SMR	P34791. Positions 97-256.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32746N.
IntAct	P34791. 3 interactions.
STRING	P34791.
2D gel databases
SWISS-2DPAGE	P34791.
Proteomic databases
PRIDE	P34791.
ProMEX	P34791.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G62030.1; AT3G62030.1; AT3G62030.
GeneID	825376.
GenomeReviews	Gene locus AT3G62030 in contig BA000014_GR.
KEGG	ath:AT3G62030.
NMPDR	fig|3702.1.peg.17585.
Organism-specific databases
GeneFarm	2619. 240.
TAIR	At3g62030.
Phylogenomic databases
eggNOG	KOG0880.
GeneTree	EPGT00070000028564.
HOGENOM	HBG610621.
InParanoid	P34791.
OMA	PWLDNRH.
PhylomeDB	P34791.
ProtClustDB	CLSN2684112.
Enzyme and pathway databases
BRENDA	5.2.1.8. 399.
Gene expression databases
ArrayExpress	P34791.
Genevestigator	P34791.
GermOnline	AT3G62030. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K03768.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
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

CP20C_ARATH

Accession

Primary (citable) accession number: P34791
Secondary accession number(s): Q8LBZ9, Q9FPH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program