P52011 (CYP3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase 3
Short name=PPIase 3
EC=5.2.1.8

Alternative name(s):
Cyclophilin-3
Rotamase 3

Gene names

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

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from sequence or structural similarity Ref.3. Source: WormBase
Cellular_component	cell Inferred from direct assay Ref.3. Source: WormBase
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.3Ref.1. Source: WormBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
K09E4.1	Q9NAP8	4	EBI-2419150,EBI-2419154

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

Turn

42 – 44

3

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

115 – 117

3

Beta strand

119 – 124

6

Helix

127 – 129

3

Turn

130 – 132

3

Beta strand

135 – 141

7

Helix

143 – 150

8

Beta strand

163 – 171

9

Sequences

	Sequence		Length	Mass (Da)
	P52011 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN A COMPLEX WITH GOLD.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

T27373.

RefSeq

NP_506751.1. NM_074350.6.

UniGene

Cel.6363.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P52011.

SMR

P52011. Positions 1-172.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52011. 1 interaction.

STRING

6239.Y75B12B.5.1.

Proteomic databases

PaxDb

P52011.

PRIDE

P52011.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

Y75B12B.5.1; Y75B12B.5.1; Y75B12B.5.
Y75B12B.5.2; Y75B12B.5.2; Y75B12B.5.

GeneID

180028.

KEGG

cel:CELE_Y75B12B.5.

UCSC

Y75B12B.5.1. c. elegans.

Organism-specific databases

CTD

180028.

WormBase

Y75B12B.5; CE20374; WBGene00000879; cyn-3.

Phylogenomic databases

eggNOG

COG0652.

GeneTree

ENSGT00690000101651.

HOGENOM

HOG000065981.

InParanoid

P52011.

KO

K01802.

OMA

FIMHKNS.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

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...

Other

EvolutionaryTrace

P52011.

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:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project