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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

  • peptidyl-prolyl cis-trans isomerase activity Source: WormBase

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-CEL-6781823. Formation of TC-NER Pre-Incision Complex.
R-CEL-6782135. Dual incision in TC-NER.
R-CEL-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-CEL-6798695. Neutrophil degranulation.
R-CEL-72163. mRNA Splicing - Major Pathway.

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
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

  • cell Source: WormBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641921 – 173Peptidyl-prolyl cis-trans isomerase 3Add BLAST173

Proteomic databases

EPDiP52011.
PaxDbiP52011.
PeptideAtlasiP52011.
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

Gene expression databases

BgeeiWBGene00000879.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiP52011. 1 interactor.
STRINGi6239.Y75B12B.5.1.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi15 – 24Combined sources10
Turni26 – 28Combined sources3
Helixi30 – 41Combined sources12
Turni42 – 44Combined sources3
Beta strandi50 – 53Combined sources4
Beta strandi62 – 64Combined sources3
Turni65 – 67Combined sources3
Beta strandi68 – 71Combined sources4
Turni74 – 76Combined sources3
Beta strandi77 – 80Combined sources4
Beta strandi104 – 107Combined sources4
Beta strandi115 – 117Combined sources3
Beta strandi119 – 124Combined sources6
Helixi127 – 129Combined sources3
Turni130 – 132Combined sources3
Beta strandi135 – 141Combined sources7
Helixi143 – 150Combined sources8
Beta strandi163 – 171Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52011.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 170PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST164

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52011.
KOiK01802.
OMAiHFRYKSA.
OrthoDBiEOG091G0BGL.
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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52011. 1 interactor.
STRINGi6239.Y75B12B.5.1.

Proteomic databases

EPDiP52011.
PaxDbiP52011.
PeptideAtlasiP52011.
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

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52011.
KOiK01802.
OMAiHFRYKSA.
OrthoDBiEOG091G0BGL.
PhylomeDBiP52011.

Enzyme and pathway databases

ReactomeiR-CEL-6781823. Formation of TC-NER Pre-Incision Complex.
R-CEL-6782135. Dual incision in TC-NER.
R-CEL-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-CEL-6798695. Neutrophil degranulation.
R-CEL-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

EvolutionaryTraceiP52011.
PROiP52011.

Gene expression databases

BgeeiWBGene00000879.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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...

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: November 30, 2016
This is version 122 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

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 one 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.