Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Keywordsi

Molecular functionIsomerase, 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000641941 – 171Peptidyl-prolyl cis-trans isomerase 7Add BLAST171

Proteomic databases

EPDiP52015.
PaxDbiP52015.
PeptideAtlasiP52015.
PRIDEiP52015.

Expressioni

Gene expression databases

BgeeiWBGene00000883.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP52015.
SMRiP52015.
ModBaseiSearch...
MobiDBiSearch...

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

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
InParanoidiP52015.
KOiK01802.
OMAiPHHAERI.
OrthoDBiEOG091G0BGL.
PhylomeDBiP52015.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiView protein in Pfam
PF00160. Pro_isomerase. 1 hit.
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti12I → T in AAC47125 (PubMed:8694762).Curated1

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.

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.

Entry informationi

Entry nameiCYP7_CAEEL
AccessioniPrimary (citable) accession number: P52015
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: July 5, 2017
This is version 124 of the entry and version 2 of the sequence. See 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