Reviewed, UniProtKB/Swiss-Prot P52011 (CYP3_CAEEL)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase 3
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-3

Gene names

Name:	cyn-3
Synonyms:	cyp-3
ORF Names:	Y75B12B.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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).
Tissue specificity	Exclusively expressed in the single anterior excretory cell. Ref.3
Developmental stage	During early larval development, peaking at the second larval stage, and dropping off in later development. Ref.3
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
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

Chain

1 – 173

173

Peptidyl-prolyl cis-trans isomerase 3

PRO_0000064192

Regions

Domain

7 – 170

164

PPIase cyclophilin-type

Secondary structure

1

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173

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

15 – 24

10

Turn

26 – 28

3

Helix

30 – 41

12

Beta strand

50 – 53

4

Beta strand

62 – 64

3

Turn

65 – 67

3

Beta strand

68 – 71

4

Turn

74 – 76

3

Beta strand

77 – 80

4

Beta strand

104 – 107

4

Beta strand

119 – 124

6

Helix

127 – 129

3

Turn

130 – 132

3

Beta strand

135 – 141

7

Helix

143 – 150

8

Sequences

	Sequence		Length	Mass (Da)
	P52011-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 39994FEF4941DEC3	FASTA	173	18,550
	10 20 30 40 50 60 MSRSKVFFDI TIGGKASGRI VMELYDDVVP KTAGNFRALC TGENGIGKSG KPLHFKGSKF 70 80 90 100 110 120 HRIIPNFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT GPGVLSMANA GPNTNGSQFF 130 140 150 160 170 LCTVKTEWLD GKHVVFGRVV EGLDVVKAVE SNGSQSGKPV KDCMIADCGQ LKA

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]	"Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans." Dornan J., Page A.P., Taylor P., Wu S., Winter A.D., Husi H., Walkinshaw M.D. J. Biol. Chem. 274:34877-34883(1999) [PubMed: 10574961] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]	"First crystal structure of a medicinally relevant gold protein complex: unexpected binding of [Au(PEt3)]+ to histidine." Zou J., Taylor P., Dornan J., Robinson S.P., Walkinshaw M.D., Sadler P.J. Angew. Chem. Int. Ed. 39:2931-2934(2000) [PubMed: 11028014] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN A COMPLEX WITH GOLD.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U31077 mRNA. Translation: AAC47129.1.
AL032663 Genomic DNA. Translation: CAA21762.1.

PIR

T27373.

RefSeq

NP_506751.1.

UniGene

Cel.6363

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DYW	X-ray	1.80	A	1-173	[»]
1E3B	X-ray	1.85	A	1-173	[»]
1E8K	X-ray	1.90	A	1-173	[»]
2IGV	X-ray	1.67	A	1-173	[»]
2IGW	X-ray	1.78	A	1-173	[»]

ModBase

Search...

Genome annotation databases

Ensembl

Y75B12B.5. Caenorhabditis elegans. [Contig view]

GeneID

180028.

KEGG

cel:Y75B12B.5.

Organism-specific databases

WormBase

WBGene00000879. cyn-3.

WormPep

Y75B12B.5. CE20374. [WorfDB]

Phylogenomic databases

OMA

P52011. VVIANCG.

Enzyme and pathway databases

BRENDA

5.2.1.8. 672.

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...

Other Resources

NextBio

907804.

Entry information

Entry name

CYP3_CAEEL

Accession

Primary (citable) accession number: P52011

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project