Reviewed, UniProtKB/Swiss-Prot Q41651 (CYPB_VICFA)

Names and origin

Protein names	Recommended name:     Peptidyl-prolyl cis-trans isomerase, chloroplastic       Short name=PPIase       Short name=Rotamase     EC=5.2.1.8 Alternative name(s):     Cyclophilin     Cyclosporin A-binding protein       Short name=CYP B
Organism	Vicia faba (Broad bean)
Taxonomic identifier	3906 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Vicia

Protein attributes

Sequence length	248 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.
Subcellular location	Plastid › chloroplast stroma.
Tissue specificity	Highly expressed in leaf.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma 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
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 248		Peptidyl-prolyl cis-trans isomerase, chloroplastic		PRO_0000025477
Regions
	Domain	85 – 243	159	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q41651-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B9688620D40AC257	FASTA	248	26,547
	10 20 30 40 50 60 MASSFSTQLV QSQNLLPRFH AVQGKPHVVS SIGCSKLSST YHYAPRLSVS QQSKAKSITS 70 80 90 100 110 120 RRITCASGAQ GEVAELQAKV TSKIFFDIEI GGESAGRIVI GLFGDAVPKT VENFKTLSTG 130 140 150 160 170 180 AKGYGYQGSF FHRIIPNFMI QGGDFTEGNG TGGVSIYGSK FEDESFDLKH VGPGVLSMAN 190 200 210 220 230 240 AGPNTNGSQF FICTVPTPWL DNRHVVFGHV IEGLDVVKQL ESQETSKLDN SPKKPCKIAK SGELPLDG

References

[1]	"pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean." Luan S., Lane W.S., Schreiber S.L. Plant Cell 6:885-892(1994) [PubMed: 8061522] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L32095 mRNA. Translation: AAA64430.1.
PIR	T12096.
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.2.1.8. 30.
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

CYPB_VICFA

Accession

Primary (citable) accession number: Q41651

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)