Reviewed, UniProtKB/Swiss-Prot P24525 (CYPH_BRANA)

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

Gene names

Name:	CYP
Synonyms:	ROT1

Organism

Brassica napus (Rape)

Taxonomic identifier

3708 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

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 – 171	171	Peptidyl-prolyl cis-trans isomerase		PRO_0000064142
Regions
	Domain	7 – 170	164	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P24525-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 4F79D3E382B57F52	FASTA	171	18,516
	10 20 30 40 50 60 MVNPKVYFDM TVGDKAAGRI VMELYADTVP ETAENFRALC TGERGIGKSG KPLHYKGSAF 70 80 90 100 110 120 HRVIPKFMCQ GGDFTAGNGT GGESIYGMKF KDENFVKKHT GPGILSMRNA GSNTNGSQFF 130 140 150 160 170 ICTEKTSWLD GKHVVFGQVV EGMDVVRDIE KVGSDSGRTS KKVVTCDCGQ L

References

[1]

"Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli." Gasser C.S., Gunning D.A., Budelier K.A., Brown S.M. Proc. Natl. Acad. Sci. U.S.A. 87:9519-9523(1990) [PubMed: 1702215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Westar.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55018 mRNA. Translation: AAA62706.1.
PIR	CSRP. B39252.
3D structure databases
SMR	P24525. Positions 1-171.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.2.1.8. 393.
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

CYPH_BRANA

Accession

Primary (citable) accession number: P24525

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	February 1, 1996
Last modified:	February 9, 2010
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)