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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

ppi1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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).

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Short name:
CPH
Cyclosporin A-binding protein
Rotamase
Gene namesi
Name:ppi1
Synonyms:cyp2
ORF Names:SPBC28F2.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC28F2.03
PomBaseiSPBC28F2.03 ppi1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641301 – 162Peptidyl-prolyl cis-trans isomeraseAdd BLAST162

Proteomic databases

MaxQBiP18253
PaxDbiP18253
PRIDEiP18253

PTM databases

iPTMnetiP18253

Interactioni

Protein-protein interaction databases

BioGridi276800, 4 interactors
STRINGi4896.SPBC28F2.03.1

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WVSmodel-A1-162[»]
ProteinModelPortaliP18253
SMRiP18253
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 161PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000065981
InParanoidiP18253
KOiK01802
OMAiEPFAVSK
OrthoDBiEOG092C5DG5
PhylomeDBiP18253

Family and domain databases

Gene3Di2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
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.

P18253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNCFFDVIA NGQPLGRIVF KLFDDVVPKT AANFRALCTG EKGYGYAGST
60 70 80 90 100
FHRVIPQFML QGGDFTRGNG TGGKSIYGEK FPDENFALKH NKPGLLSMAN
110 120 130 140 150
AGPNTNGSQF FITTVVTPWL DGKHVVFGEV TEGMDVVKKV ESLGSNSGAT
160
RARIVIDKCG TV
Length:162
Mass (Da):17,402
Last modified:November 1, 1990 - v1
Checksum:iB9F3747B7710C46E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53223 Genomic DNA Translation: CAA37322.1
D83992 Genomic DNA Translation: BAA12183.1
CU329671 Genomic DNA Translation: CAB57932.1
PIRiS11212 CSZPA
RefSeqiNP_595664.1, NM_001021559.2

Genome annotation databases

EnsemblFungiiSPBC28F2.03.1; SPBC28F2.03.1:pep; SPBC28F2.03
GeneIDi2540269
KEGGispo:SPBC28F2.03

Similar proteinsi

Entry informationi

Entry nameiCYPH_SCHPO
AccessioniPrimary (citable) accession number: P18253
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: March 28, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health