Reviewed, UniProtKB/Swiss-Prot P52013 (CYP5_CAEEL)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase 5
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-5

Gene names

Name:	cyn-5
Synonyms:	cyp-5
ORF Names:	F31C3.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	204 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). Ref.3
Subcellular location	Cytoplasm Ref.3.
Tissue specificity	Embryonic, larval and adult gut cells. Ref.3
Developmental stage	Throughout development, highest in embryos. Ref.3
Induction	Inhibited by cyclosporin. Ref.3
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.
Mass spectrometry	Molecular mass is 20766 Da from positions 23 - 204. Determined by MALDI. Ref.3

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Signal
Molecular function	Isomerase Rotamase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
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	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

Signal peptide

1 – 22

22

Ref.3

Chain

23 – 204

182

Peptidyl-prolyl cis-trans isomerase 5

PRO_0000025495

Regions

Domain

32 – 189

158

PPIase cyclophilin-type

Amino acid modifications

Glycosylation

133

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

4 – 18

15

LLVVA…GALAQ → FLLWRPCSLSELLLR in AAC47126. Ref.1

Secondary structure

1

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204

Helix Strand Turn

Details...

Beta strand

26 – 37

12

Beta strand

40 – 49

10

Turn

51 – 53

3

Helix

55 – 66

12

Turn

69 – 71

3

Beta strand

80 – 82

3

Turn

83 – 85

3

Beta strand

86 – 89

4

Turn

92 – 94

3

Beta strand

95 – 98

4

Beta strand

122 – 125

4

Beta strand

137 – 142

6

Helix

145 – 147

3

Turn

148 – 150

3

Beta strand

153 – 159

7

Helix

161 – 168

8

Turn

174 – 176

3

Beta strand

177 – 180

4

Beta strand

182 – 197

16

Sequences

	Sequence		Length	Mass (Da)
	P52013-1 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: 6216192BFE1FB493	FASTA	204	21,927
	10 20 30 40 50 60 MKSLLVVAAV LAVGALAQGD DAKGPKVTDK VYFDMEIGGK PIGRIVIGLF GKTVPKTATN 70 80 90 100 110 120 FIELAKKPKG EGYPGSKFHR VIADFMIQGG DFTRGDGTGG RSIYGEKFAD ENFKLKHYGA 130 140 150 160 170 180 GWLSMANAGA DTNGSQFFIT TVKTPWLDGR HVVFGKILEG MDVVRKIEQT EKLPGDRPKQ 190 200 DVIIAASGHI AVDTPFSVER EAVV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans." Page A.P., Macniven K., Hengartner M.O. Biochem. J. 317:179-185(1996) [PubMed: 8694762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans." Picken N.C., Eschenlauer S., Taylor P., Page A.P., Walkinshaw M.D. J. Mol. Biol. 322:15-25(2002) [PubMed: 12215411] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-27, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-204, MASS SPECTROMETRY, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31948 mRNA. Translation: AAC47126.1.
Z92784 Genomic DNA. Translation: CAB07192.1.

PIR

T21587.

RefSeq

NP_493624.1.

UniGene

Cel.6652

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H0P	X-ray	1.75	A	23-204	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P52013. 1 interaction.

Genome annotation databases

Ensembl

F31C3.1.1; F31C3.1.1; F31C3.1; Caenorhabditis elegans. [Genome view]
F31C3.1.2; F31C3.1.2; F31C3.1; Caenorhabditis elegans. [Genome view]

GeneID

173374.

KEGG

cel:F31C3.1.

UCSC

F31C3.1.1. c. elegans.

Organism-specific databases

CTD

173374.

WormBase

WBGene00000881. cyn-5.

WormPep

F31C3.1. CE17730. [WorfDB]

Phylogenomic databases

eggNOG

meNOG10184.

HOGENOM

HBG610621.

InParanoid

P52013.

OMA

KGPKVTA.

PhylomeDB

P52013.

Enzyme and pathway databases

BRENDA

5.2.1.8. 672.

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...

Other Resources

NextBio

879385.

Entry information

Entry name

CYP5_CAEEL

Accession

Primary (citable) accession number: P52013
Secondary accession number(s): O62190

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	June 20, 2003
Last modified:	January 19, 2010
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project