Reviewed, UniProtKB/Swiss-Prot P35627 (CYPX_USEUD)

Names and origin

Protein names	Recommended name:     Peptidyl-prolyl cis-trans isomerase       Short name=PPIase       Short name=Rotamase     EC=5.2.1.8 Alternative name(s):     Cyclophilin     Cyclosporin A-binding protein
Organism	Unspecified eudicot DB-1992
Taxonomic identifier	323200 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.
Caution	Was originally (Ref.1) reported to be isolated from an A.thaliana cDNA library. Ref.2 authors have assigned that the sequence has been amplified from an other contaminating organism.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 169	169	Peptidyl-prolyl cis-trans isomerase		PRO_0000064139
Regions
	Domain	5 – 168	164	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P35627-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: B6077FC139864931	FASTA	169	18,161
	10 20 30 40 50 60 MAHCFFDMTI GGQPAGRIIM ELFPDVPKTA ENFRALCTGE KGIGPSGKKM TYEGSVFHRV 70 80 90 100 110 120 IPKFMLQGGD FTLGNGRGGE SIYGAKFADE NFIHKHTTPG LLSMANAGPG TNGSQFFITT 130 140 150 160 VATPHLDGKH VVFGKVVEGM DVVRKIEATQ TDRGDKPLSE VKIAKCGQL

References

[1]	"Nucleotide sequence of a cDNA encoding an Arabidopsis cyclophilin-like protein." Bartling D., Heese A., Weiler E.W. Plant Mol. Biol. 19:529-530(1992) [PubMed: 1623198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: DISCUSSION OF ORIGIN OF SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63616 mRNA. Translation: CAA45161.1.
PIR	S22496.
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
ModBase	Search...
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

CYPX_USEUD

Accession

Primary (citable) accession number: P35627

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)