Reviewed, UniProtKB/Swiss-Prot Q38867 (CP19C_ARATH)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase CYP19-3
      Short name=PPIase CYP19-3
    EC=5.2.1.8
Alternative name(s):
    Rotamase cyclophilin-2
    Cyclophilin of 19 kDa 3
    Cyclophilin-4

Gene names

Name:	CYP19-3
Synonyms:	CYP4, ROC2
Ordered Locus Names:	At3g56070
ORF Names:	F18O21.30

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	176 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.
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	Ubiquitous, with highest levels in flowers and lowest levels in roots. Ref.1 Ref.5
Induction	By wounding, and slightly by light. Ref.1
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 response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	cytoplasm 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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAM1	P25854	1	EBI-1235851,EBI-1235664
CAM6	Q03509	1	EBI-1235851,EBI-1236097
CAM7	P59220	1	EBI-1235851,EBI-1236031
CML9	Q9S744	1	EBI-1235851,EBI-1236048

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	Peptidyl-prolyl cis-trans isomerase CYP19-3		PRO_0000064137
Regions
	Domain	7 – 170	164	PPIase cyclophilin-type
Experimental info
	Sequence conflict	155	1	D → Y in AAA74096. Ref.2
	Sequence conflict	172	1	K → N in AAB96833. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q38867-1 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 24C2031B6CB4DD90	FASTA	176	18,921
	10 20 30 40 50 60 MANPKVFFDI LIGKMKAGRV VMELFADVTP RTANNFRALC TGENGIGKAG KALHYKGSAF 70 80 90 100 110 120 HRIIPGFMCQ GGDFTRGNGT GGESIYGSKF EDENFKLKHT GPGILSMANS GPNTNGSQFF 130 140 150 160 170 ICTEKTSWLD GKHVVFGKVV DGYNVVKAME DVGSDMGNPS ERVVIEDCGE LKNPSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[2]	Saito T., Ashida H., Kawamukai M., Matsuda H., Nakagawa T. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[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]	"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]	"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	U40400 Genomic DNA. Translation: AAB96833.1. U31370 Genomic DNA. Translation: AAA74096.1. AL163763 Genomic DNA. Translation: CAB87406.1. AY072128 mRNA. Translation: AAL59950.1. AY096697 mRNA. Translation: AAM20331.1.
IPI	IPI00520711.
PIR	T47724. T50767.
RefSeq	NP_001078301.1. NP_191166.1.
UniGene	At.34965
3D structure databases
SMR	Q38867. Positions 1-172.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q38867. 4 interactions.
STRING	Q38867.
Proteomic databases
PRIDE	Q38867.
Genome annotation databases
GeneID	824773.
GenomeReviews	Gene locus AT3G56070 in contig BA000014_GR.
KEGG	ath:AT3G56070.
NMPDR	fig|3702.1.peg.16931.
Organism-specific databases
TAIR	At3g56070.
Phylogenomic databases
eggNOG	KOG0865.
HOGENOM	HBG610621.
InParanoid	Q38867.
OMA	FFDILIG.
PhylomeDB	Q38867.
Enzyme and pathway databases
BRENDA	5.2.1.8. 302.
Gene expression databases
Genevestigator	Q38867.
GermOnline	AT3G56070. 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

CP19C_ARATH

Accession

Primary (citable) accession number: Q38867
Secondary accession number(s): Q38901, Q9LYN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	February 9, 2010
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)