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Protein

Peptidyl-prolyl cis-trans isomerase 3

Gene

cyn-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: WormBase

GO - Biological processi

  1. protein folding Source: WormBase
  2. protein peptidyl-prolyl isomerization Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase 3 (EC:5.2.1.8)
Short name:
PPIase 3
Alternative name(s):
Cyclophilin-3
Rotamase 3
Gene namesi
Name:cyn-3
Synonyms:cyp-3
ORF Names:Y75B12B.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome V

Organism-specific databases

WormBaseiY75B12B.5; CE20374; WBGene00000879; cyn-3.

Subcellular locationi

GO - Cellular componenti

  1. cell Source: WormBase
  2. mitochondrion Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Peptidyl-prolyl cis-trans isomerase 3PRO_0000064192Add
BLAST

Proteomic databases

PaxDbiP52011.
PRIDEiP52011.

Expressioni

Tissue specificityi

Exclusively expressed in the single anterior excretory cell.1 Publication

Developmental stagei

During early larval development, peaking at the second larval stage, and dropping off in later development.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CELE_K09E4.1Q9NAP84EBI-2419150,EBI-2419154

Protein-protein interaction databases

IntActiP52011. 1 interaction.
STRINGi6239.Y75B12B.5.1.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi15 – 2410Combined sources
Turni26 – 283Combined sources
Helixi30 – 4112Combined sources
Turni42 – 443Combined sources
Beta strandi50 – 534Combined sources
Beta strandi62 – 643Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 714Combined sources
Turni74 – 763Combined sources
Beta strandi77 – 804Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi119 – 1246Combined sources
Helixi127 – 1293Combined sources
Turni130 – 1323Combined sources
Beta strandi135 – 1417Combined sources
Helixi143 – 1508Combined sources
Beta strandi163 – 1719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYWX-ray1.80A1-173[»]
1E3BX-ray1.85A1-173[»]
1E8KX-ray1.90A1-173[»]
2IGVX-ray1.67A1-173[»]
2IGWX-ray1.78A1-173[»]
ProteinModelPortaliP52011.
SMRiP52011. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52011.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 170164PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated
Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52011.
KOiK01802.
OMAiHPKVFFD.
OrthoDBiEOG79GT7W.
PhylomeDBiP52011.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52011-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRSKVFFDI TIGGKASGRI VMELYDDVVP KTAGNFRALC TGENGIGKSG
60 70 80 90 100
KPLHFKGSKF HRIIPNFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT
110 120 130 140 150
GPGVLSMANA GPNTNGSQFF LCTVKTEWLD GKHVVFGRVV EGLDVVKAVE
160 170
SNGSQSGKPV KDCMIADCGQ LKA
Length:173
Mass (Da):18,550
Last modified:October 1, 1996 - v1
Checksum:i39994FEF4941DEC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31077 mRNA. Translation: AAC47129.1.
AL032663 Genomic DNA. Translation: CAA21762.1.
PIRiT27373.
RefSeqiNP_506751.1. NM_074350.6.
UniGeneiCel.6363.

Genome annotation databases

EnsemblMetazoaiY75B12B.5; Y75B12B.5; WBGene00000879.
GeneIDi180028.
KEGGicel:CELE_Y75B12B.5.
UCSCiY75B12B.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31077 mRNA. Translation: AAC47129.1.
AL032663 Genomic DNA. Translation: CAA21762.1.
PIRiT27373.
RefSeqiNP_506751.1. NM_074350.6.
UniGeneiCel.6363.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYWX-ray1.80A1-173[»]
1E3BX-ray1.85A1-173[»]
1E8KX-ray1.90A1-173[»]
2IGVX-ray1.67A1-173[»]
2IGWX-ray1.78A1-173[»]
ProteinModelPortaliP52011.
SMRiP52011. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52011. 1 interaction.
STRINGi6239.Y75B12B.5.1.

Proteomic databases

PaxDbiP52011.
PRIDEiP52011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY75B12B.5; Y75B12B.5; WBGene00000879.
GeneIDi180028.
KEGGicel:CELE_Y75B12B.5.
UCSCiY75B12B.5.1. c. elegans.

Organism-specific databases

CTDi180028.
WormBaseiY75B12B.5; CE20374; WBGene00000879; cyn-3.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52011.
KOiK01802.
OMAiHPKVFFD.
OrthoDBiEOG79GT7W.
PhylomeDBiP52011.

Miscellaneous databases

EvolutionaryTraceiP52011.
NextBioi907804.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCYP3_CAEEL
AccessioniPrimary (citable) accession number: P52011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.