cyclophilin E (cyclophilin 3, 33kD peptidyl-prolyl cis-trans isomerase, cyclophilin 33, rotamase E, PPIE, CYP33)

Function: - PPIases accelerate the folding of proteins - catalyzes cis-trans isomerization of proline imidic peptide bonds in oligopeptides - combines RNA-binding & PPIase activities - may be involved in muscle- & brain-specific processes - may be involved in pre-mRNA splicing - identified in the spliceosome C complex peptidylproline (omega=180) peptidylproline (omega=0) Structure: - belongs to the cyclophilin-type PPIase family, PPIase E subfamily - contains 1 PPIase cyclophilin-type domain contains 1 RRM (RNA recognition motif) domain Compartment: nucleus Alternative splicing: named isoforms=2 Expression: - found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney & pancreas

General

chaperonin; chaperone cyclophilin

Properties

SIZE: entity length = 301 aa MW = 33 kD COMPARTMENT: cell nucleus MOTIF: RNP motif NAME: RNP motif SITE: 6-84 FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif NAME: ribonucleoprotein-1 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif ribonucleoprotein-2 motif FOR-BINDING-OF: ribonucleic acid MOTIF: ribonucleoprotein-1 motif ribonucleoprotein-2 motif alanine-rich region {60-63} MOTIF: alanine residue (SEVERAL) active site SITE: 143-299

Database Correlations

OMIM 602435 UniProt Q9UNP9 Entrez Gene 10450 ENZYME 5.2.1.8

References

UniProt :accession Q9UNP9