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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: Annotation score: 4 out of 5-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

  • peptide binding Source: UniProtKB-KW
  • peptidyl-prolyl cis-trans isomerase activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

ReactomeiR-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-6798695. Neutrophil degranulation.

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

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiP18253.
PRIDEiP18253.

Interactioni

Protein-protein interaction databases

BioGridi276800. 4 interactors.
MINTiMINT-4687510.

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

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000065981.
InParanoidiP18253.
KOiK01802.
OMAiITRAGNA.
OrthoDBiEOG092C5DG5.
PhylomeDBiP18253.

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.

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.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

BioGridi276800. 4 interactors.
MINTiMINT-4687510.

Proteomic databases

MaxQBiP18253.
PRIDEiP18253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPBC28F2.03.
PomBaseiSPBC28F2.03. ppi1.

Phylogenomic databases

HOGENOMiHOG000065981.
InParanoidiP18253.
KOiK01802.
OMAiITRAGNA.
OrthoDBiEOG092C5DG5.
PhylomeDBiP18253.

Enzyme and pathway databases

ReactomeiR-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP18253.

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...

Entry informationi

Entry nameiCYPH_SCHPO
AccessioniPrimary (citable) accession number: P18253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 30, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.