Reviewed, UniProtKB/Swiss-Prot Q9SP02 (CP20A_ARATH)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase CYP20-1
      Short name=PPIase CYP20-1
    EC=5.2.1.8
Alternative name(s):
    Rotamase cyclophilin-7
    Cyclophilin of 20 kDa 1

Gene names

Name:	CYP20-1
Synonyms:	ROC7
Ordered Locus Names:	At5g58710
ORF Names:	MZN1.15

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	204 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. Seems to be involved in root development. Ref.1
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 By similarity.
Subunit structure	Interacts with the PP2A A subunit PP2AA1/RCN1. Ref.1
Subcellular location	Endoplasmic reticulum By similarity. Secreted By similarity.
Tissue specificity	Ubiquitous, mostly in aerial organs. Higher levels in leaf and buds, and lower levels in seedlings. Ref.1 Ref.5
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Secreted
Domain	Signal
Ligand	Cyclosporin
Molecular function	Chaperone Isomerase Rotamase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW root development Ref.1 Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 204	181	Peptidyl-prolyl cis-trans isomerase CYP20-1		PRO_0000044627
Regions
	Domain	38 – 201	164	PPIase cyclophilin-type
Experimental info
	Mutagenesis	124 – 128	5	ENFKL → AAFAA or KNFEL: Reduced interaction with PP2AA1/RCN1. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SP02-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CE2967AB4F65AF44	FASTA	204	21,961
	10 20 30 40 50 60 MASSVTLLLW SLLLLGTLSA IQAKKSKENL KEITHKVYFD VEIDGKAAGR IVMGLFGKTV 70 80 90 100 110 120 PKTVENFRAL CTGEKGIGKN GKALHYKGSS FHRIIPSFML QGGDFTHGNG MGGESIYGEK 130 140 150 160 170 180 FADENFKLKH TGPGFLSMAN AGQDTNGSQF FITTVTTSWL DGRHVVFGKV VTGMDVVYKV 190 200 EAEGNQSGTP KSKVVIVDSG ELPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2A." Jackson K., Soell D. Mol. Gen. Genet. 262:830-838(1999) [PubMed: 10628867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PP2AA1/RCN1, MUTAGENESIS OF 124-GLU--LEU-128. Strain: cv. Wassilewskija.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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.
[4]	"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].
[5]	"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.
[6]	"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	AF192490 mRNA. Translation: AAF05760.1. AB020755 Genomic DNA. Translation: BAA97339.1. AY048227 mRNA. Translation: AAK82490.1. AY094017 mRNA. Translation: AAM16173.1. AY086471 mRNA. Translation: AAM63473.1.
IPI	IPI00522741.
PIR	T50838.
RefSeq	NP_200679.1.
UniGene	At.49190 At.7874
3D structure databases
SMR	Q9SP02. Positions 36-202.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SP02.
Proteomic databases
PRIDE	Q9SP02.
Genome annotation databases
GeneID	835985.
GenomeReviews	Gene locus AT5G58710 in contig BA000015_GR.
KEGG	ath:AT5G58710.
NMPDR	fig|3702.1.peg.27855.
Organism-specific databases
GeneFarm	5176.
TAIR	At5g58710.
Phylogenomic databases
eggNOG	KOG0865.
HOGENOM	HBG610621.
InParanoid	Q9SP02.
OMA	VYKVEAE.
PhylomeDB	Q9SP02.
Enzyme and pathway databases
BRENDA	5.2.1.8. 302.
Gene expression databases
Genevestigator	Q9SP02.
GermOnline	AT5G58710. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR015891. Cyclophilin-like. IPR020892. Pep-Pro_Isoase_cyclophilin_CS. IPR002130. PPIase_cyclophilin. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP20A_ARATH

Accession

Primary (citable) accession number: Q9SP02

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)