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P52011

- CYP3_CAEEL

UniProt

P52011 - CYP3_CAEEL

Protein

Peptidyl-prolyl cis-trans isomerase 3

Gene

cyn-3

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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
    2. protein binding Source: IntAct

    GO - Biological processi

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

    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

    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 – 128
    Beta strandi15 – 2410
    Turni26 – 283
    Helixi30 – 4112
    Turni42 – 443
    Beta strandi50 – 534
    Beta strandi62 – 643
    Turni65 – 673
    Beta strandi68 – 714
    Turni74 – 763
    Beta strandi77 – 804
    Beta strandi104 – 1074
    Beta strandi115 – 1173
    Beta strandi119 – 1246
    Helixi127 – 1293
    Turni130 – 1323
    Beta strandi135 – 1417
    Helixi143 – 1508
    Beta strandi163 – 1719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00750000117619.
    HOGENOMiHOG000065981.
    InParanoidiP52011.
    KOiK01802.
    OMAiNFAKKHE.
    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

    MSRSKVFFDI TIGGKASGRI VMELYDDVVP KTAGNFRALC TGENGIGKSG    50
    KPLHFKGSKF HRIIPNFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT 100
    GPGVLSMANA GPNTNGSQFF LCTVKTEWLD GKHVVFGRVV EGLDVVKAVE 150
    SNGSQSGKPV KDCMIADCGQ LKA 173
    Length:173
    Mass (Da):18,550
    Last modified:October 1, 1996 - v1
    Checksum:i39994FEF4941DEC3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31077 mRNA. Translation: AAC47129.1 .
    AL032663 Genomic DNA. Translation: CAA21762.1 .
    PIRi T27373.
    RefSeqi NP_506751.1. NM_074350.6.
    UniGenei Cel.6363.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P52011.
    SMRi P52011. Positions 1-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P52011. 1 interaction.
    STRINGi 6239.Y75B12B.5.1.

    Proteomic databases

    PaxDbi P52011.
    PRIDEi P52011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai Y75B12B.5 ; Y75B12B.5 ; WBGene00000879 .
    GeneIDi 180028.
    KEGGi cel:CELE_Y75B12B.5.
    UCSCi Y75B12B.5.1. c. elegans.

    Organism-specific databases

    CTDi 180028.
    WormBasei Y75B12B.5 ; CE20374 ; WBGene00000879 ; cyn-3.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00750000117619.
    HOGENOMi HOG000065981.
    InParanoidi P52011.
    KOi K01802.
    OMAi NFAKKHE.
    OrthoDBi EOG79GT7W.
    PhylomeDBi P52011.

    Miscellaneous databases

    EvolutionaryTracei P52011.
    NextBioi 907804.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 102 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