Q9ASS6 (CP20B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP20-2, chloroplastic
Short name=PPIase CYP20-2
EC=5.2.1.8

Alternative name(s):
Cyclophilin of 20 kDa 2
Rotamase CYP20-2
Thylakoid lumen PPIase of 20 kDa
Short name=TLP20

Gene names

Name:	CYP20-2
Ordered Locus Names:	At5g13120
ORF Names:	T19L5_80

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	259 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 By similarity.
Subunit structure	Interacts with AHK2. Ref.10
Subcellular location	Plastid › chloroplast thylakoid lumen. Plastid › chloroplast membrane; Peripheral membrane protein. Note: Peripherally associated with PSII complexes. Ref.6 Ref.7 Ref.8 Ref.9
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.
Sequence caution	The sequence CAC05440.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Membrane Plastid Thylakoid
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	NAD(P)H dehydrogenase complex assembly Inferred from mutant phenotype. Source: TAIR protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast membrane Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast stromal thylakoid Inferred from direct assay. Source: TAIR chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast thylakoid membrane 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 mutant phenotype. Source: TAIR protein histidine kinase binding Inferred from physical interaction Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHK2	Q9C5U2	2	EBI-1807485,EBI-1100634

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: Q9ASS6-1)

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 – ?		Chloroplast Potential
	Transit peptide	? – 76		Thylakoid Ref.6
	Chain	77 – 259	183	Peptidyl-prolyl cis-trans isomerase CYP20-2, chloroplastic		PRO_0000025503
Regions
	Domain	96 – 253	158	PPIase cyclophilin-type
Amino acid modifications
	Disulfide bond	204 ↔ 251		By similarity
Experimental info
	Sequence conflict	29	1	F → L in AAM65904. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 7EDD221E80708BE2	FASTA	259	28,306
	10 20 30 40 50 60 MATLSMTLSN PKSLSAPPRR LSPINTSAFT STSFRLRTKS SFDSISFSSS TPFSASSLLL 70 80 90 100 110 120 HTSYTKRNHR CFSVQSNAEV VTEPQSKITH KVYFDISVGN PVGKLAGRIV IGLYGDDVPQ 130 140 150 160 170 180 TVENFRALCT GEKGFGYKGS TFHRVIRDFM IQGGDFEKGN GTGGKSVYGR TFKDENFKLS 190 200 210 220 230 240 HVGPGVLSMA NAGPNTNGSQ FFICTIKTSW LDGRHVVFGQ VIEGMEVVKL IEEQETDRGD 250 RPRKKVVIAD CGQLPMSEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [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]	"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: PROTEIN SEQUENCE OF 77-88, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction." Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G., Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G., van Wijk K.J. Plant Cell 14:211-236(2002) [PubMed: 11826309] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"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.
[9]	"Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes." Romano P.G.N., Edvardsson A., Ruban A.V., Andersson B., Vener A.V., Gray J.E., Horton P. Plant Physiol. 134:1244-1247(2004) [PubMed: 15084723] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Toward an interaction map of the two-component signaling pathway of Arabidopsis thaliana." Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A. J. Proteome Res. 7:3649-3660(2008) [PubMed: 18642946] [Abstract] Cited for: INTERACTION WITH AHK2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY568517 mRNA. Translation: AAS75300.1. AL391711 Genomic DNA. Translation: CAC05440.1. Sequence problems. CP002688 Genomic DNA. Translation: AED91852.1. AF367307 mRNA. Translation: AAK32894.1. AY059152 mRNA. Translation: AAL15377.1. AY088365 mRNA. Translation: AAM65904.1.
IPI	IPI00540014.
RefSeq	NP_196816.1. NM_121315.2.
UniGene	At.10074. At.67814.
3D structure databases
ProteinModelPortal	Q9ASS6.
SMR	Q9ASS6. Positions 92-254.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ASS6. 2 interactions.
STRING	Q9ASS6.
Proteomic databases
PRIDE	Q9ASS6.
ProMEX	Q9ASS6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G13120.1; AT5G13120.1; AT5G13120.
GeneID	831151.
GenomeReviews	Gene locus AT5G13120 in contig BA000015_GR.
KEGG	ath:AT5G13120.
NMPDR	fig|3702.1.peg.23427.
Organism-specific databases
GeneFarm	2251. 240.
TAIR	At5g13120.
Phylogenomic databases
eggNOG	KOG0880.
GeneTree	EPGT00070000028564.
HOGENOM	HBG610621.
InParanoid	Q9ASS6.
OMA	DISIGNP.
PhylomeDB	Q9ASS6.
ProtClustDB	CLSN2916504.
Gene expression databases
ArrayExpress	Q9ASS6.
Genevestigator	Q9ASS6.
GermOnline	AT5G13120. 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

CP20B_ARATH

Accession

Primary (citable) accession number: Q9ASS6
Secondary accession number(s): Q53YK9, Q8L9L5, Q9FY98

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program