P34887 (CYPH_ALLCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
EC=5.2.1.8

Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Rotamase

Gene names

Name:

CYP

Organism

Allium cepa (Onion)

Taxonomic identifier

4679 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Asparagales › Amaryllidaceae › Allioideae › Allieae › Allium

Protein attributes

Sequence length	150 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 By similarity.
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 – 150	150	Peptidyl-prolyl cis-trans isomerase		PRO_0000064140
Regions
	Domain	1 – 148	148	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P34887 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 9223D16840F7E241	FASTA	150	16,033
	10 20 30 40 50 60 MELFQDVVPQ TAENFRALCT GEKGMGDRKP LHYKGSSFHR VIPGFMCQGG DFTAGNGTGG 70 80 90 100 110 120 ESIYGAKFKD ENFIKKHTGP GVLSMANAGP GTNGSQFFIC TEKTAWLDGK HVVFGQVVEG 130 140 150 MDVVRAIEKV GSQSGQTKKP VKIADCGQLS

References

[1]	Clark S.A. Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13365 mRNA. Translation: AAA32642.1.
3D structure databases
ProteinModelPortal	P34887.
SMR	P34887. Positions 1-149.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPH_ALLCE

Accession

Primary (citable) accession number: P34887

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program