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Protein

Peptidyl-prolyl cis-trans isomerase 7

Gene

cyn-7

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase 7 (EC:5.2.1.8)
Short name:
PPIase 7
Alternative name(s):
Cyclophilin-7
Rotamase 7
Gene namesi
Name:cyn-7
Synonyms:cyp-7
ORF Names:Y75B12B.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiY75B12B.2; CE20371; WBGene00000883; cyn-7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171Peptidyl-prolyl cis-trans isomerase 7PRO_0000064194Add
BLAST

Proteomic databases

EPDiP52015.
PaxDbiP52015.
PeptideAtlasiP52015.
PRIDEiP52015.

Interactioni

Protein-protein interaction databases

BioGridi45022. 1 interaction.
DIPiDIP-24704N.
MINTiMINT-1105763.
STRINGi6239.Y75B12B.2.2.

Structurei

3D structure databases

ProteinModelPortaliP52015.
SMRiP52015. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52015.
KOiK01802.
OMAiGRPHVFF.
PhylomeDBiP52015.

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.

P52015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPRVFFDI TIAGKPTGRI VMELYNDIVP KTAENFRALC TGEKGVGKSG
60 70 80 90 100
KPLHFKGSKF HRIIPEFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT
110 120 130 140 150
GPGVLSMANA GPNTNGSQFF LCTVKTAWLD GKHVVFGRVV EGLDIVSKVE
160 170
GNGSSSGTPK SECLIADCGQ L
Length:171
Mass (Da):18,401
Last modified:December 1, 2000 - v2
Checksum:iD5BD5E32A32942A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121I → T in AAC47125 (PubMed:8694762).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27559 mRNA. Translation: AAC47125.1.
AL032663 Genomic DNA. Translation: CAA21760.1.
PIRiT27371.
RefSeqiNP_506749.1. NM_074348.7.
UniGeneiCel.6641.

Genome annotation databases

EnsemblMetazoaiY75B12B.2.1; Y75B12B.2.1; WBGene00000883.
Y75B12B.2.2; Y75B12B.2.2; WBGene00000883.
GeneIDi180027.
KEGGicel:CELE_Y75B12B.2.
UCSCiY75B12B.2.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27559 mRNA. Translation: AAC47125.1.
AL032663 Genomic DNA. Translation: CAA21760.1.
PIRiT27371.
RefSeqiNP_506749.1. NM_074348.7.
UniGeneiCel.6641.

3D structure databases

ProteinModelPortaliP52015.
SMRiP52015. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45022. 1 interaction.
DIPiDIP-24704N.
MINTiMINT-1105763.
STRINGi6239.Y75B12B.2.2.

Proteomic databases

EPDiP52015.
PaxDbiP52015.
PeptideAtlasiP52015.
PRIDEiP52015.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY75B12B.2.1; Y75B12B.2.1; WBGene00000883.
Y75B12B.2.2; Y75B12B.2.2; WBGene00000883.
GeneIDi180027.
KEGGicel:CELE_Y75B12B.2.
UCSCiY75B12B.2.1. c. elegans.

Organism-specific databases

CTDi180027.
WormBaseiY75B12B.2; CE20371; WBGene00000883; cyn-7.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52015.
KOiK01802.
OMAiGRPHVFF.
PhylomeDBiP52015.

Miscellaneous databases

PROiP52015.

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...

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. "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing."
    Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.
    Electrophoresis 18:557-562(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13.
    Strain: Bristol N2.

Entry informationi

Entry nameiCYP7_CAEEL
AccessioniPrimary (citable) accession number: P52015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. 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.