Reviewed, UniProtKB/Swiss-Prot Q9SKQ0 (CP19B_ARATH)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase CYP19-2
      Short name=PPIase CYP19-2
    EC=5.2.1.8
Alternative name(s):
    Rotamase cyclophilin-6
    Cyclophilin of 19 kDa 2
      Short name=Cyclophilin-2

Gene names

Name:	CYP19-2
Synonyms:	CYP2, ROC6
Ordered Locus Names:	At2g21130
ORF Names:	F26H11.11

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm Probable.
Tissue specificity	Pollen (at protein level). Widely expressed in aerial organs, at high levels in young rosette leaves and flowers, at low levels in older tissues. Ref.4 Ref.5 Ref.7 Ref.8
Developmental stage	Mostly expressed in young tissues. Expressed in all parts of floral buds, but later confined to stigma and anthers. Ref.4
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell 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 – 174	174	Peptidyl-prolyl cis-trans isomerase CYP19-2		PRO_0000064136
Regions
	Domain	8 – 171	164	PPIase cyclophilin-type
Experimental info
	Sequence conflict	166	1	I → V in AAB71402. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SKQ0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6D322CB197ABC7AF	FASTA	174	18,464
	10 20 30 40 50 60 MASHPKVFFD MTIGGAPAGK IVMELYTDKT PKTAENFRAL CTGEKGVGRS GKPLHFKGSS 70 80 90 100 110 120 FHRVIPNFMC QGGDFTKGNG TGGESIYGAK FEDENFERKH TGPGILSMAN AGANTNGSQF 130 140 150 160 170 FICTVKTDWL DGKHVVFGQV VEGLDVVKAI EKIGSSSGKP TKPVVIADCG EISS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of genes for cyclophilin from Arabidopsis thaliana." Saito T., Ishiguro S., Ashida H., Kawamukai M., Matsuda H., Ochiai H., Nakagawa T. Plant Cell Physiol. 36:377-382(1995) [PubMed: 7767603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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].
[4]	"Two cytosolic cyclophilin genes of Arabidopsis thaliana differently regulated in temporal- and organ-specific expression." Saito T., Tadakuma K., Takahashi N., Ashida H., Tanaka K., Kawamukai M., Matsuda H., Nakagawa T. Biosci. Biotechnol. Biochem. 63:632-637(1999) [PubMed: 10361676] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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.
[7]	"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.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF020434 Genomic DNA. Translation: AAB71402.1. AC006264 Genomic DNA. Translation: AAD29803.1. AY087454 mRNA. Translation: AAM65000.1.
IPI	IPI00537930.
PIR	E84597. T50772.
RefSeq	NP_179709.1.
UniGene	At.10399
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
SMR	Q9SKQ0. Positions 3-172.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SKQ0.
Proteomic databases
PRIDE	Q9SKQ0.
ProMEX	Q9SKQ0.
Genome annotation databases
GeneID	816648.
GenomeReviews	Gene locus AT2G21130 in contig CT485783_GR.
KEGG	ath:AT2G21130.
NMPDR	fig|3702.1.peg.9132.
Organism-specific databases
TAIR	At2g21130.
Phylogenomic databases
OMA	VVIANCG.
Enzyme and pathway databases
BRENDA	5.2.1.8. 302.
Gene expression databases
ArrayExpress	Q9SKQ0.
Genevestigator	Q9SKQ0.
GermOnline	AT2G21130. Arabidopsis thaliana.
Family and domain databases
InterPro	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

CP19B_ARATH

Accession

Primary (citable) accession number: Q9SKQ0
Secondary accession number(s): O22516

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)