Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P18253 (CYPH_SCHPO)

Last modified November 3, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
      Short name=CPH
    Cyclosporin A-binding protein
Gene names
Name: ppi1
Synonyms: cyp2
ORF Names: SPBC28F2.03
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Hide | Top

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Hide | Top

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Peptidyl-prolyl cis-trans isomerase
PRO_0000064130

Regions

Domain5 – 161157PPIase cyclophilin-type

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P18253-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: B9F3747B7710C46E

FASTA16217,402
        10         20         30         40         50         60 
MSNCFFDVIA NGQPLGRIVF KLFDDVVPKT AANFRALCTG EKGYGYAGST FHRVIPQFML 

        70         80         90        100        110        120 
QGGDFTRGNG TGGKSIYGEK FPDENFALKH NKPGLLSMAN AGPNTNGSQF FITTVVTPWL 

       130        140        150        160 
DGKHVVFGEV TEGMDVVKKV ESLGSNSGAT RARIVIDKCG TV

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"The gene for cyclophilin (peptidyl-prolyl cis-trans isomerase) from Schizosaccharomyces pombe."
de Martin R., Philipson L.
Nucleic Acids Res. 18:4917-4917(1990) [PubMed: 2204030] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"S.pombe chromosome II cosmid 1228 sequence."
Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K., Yanagida M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38366 / 972.
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Hide | Top

Cross-references

Sequence databases

X53223 Genomic DNA. Translation: CAA37322.1.
D83992 Genomic DNA. Translation: BAA12183.1.
CU329671 Genomic DNA. Translation: CAB57932.1.
PIRCSZPA. S11212.
RefSeqNP_595664.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WVSmodel-A1-162[»]
SMRP18253. Positions 1-160.
ModBaseSearch...

Protein-protein interaction databases

STRINGP18253.

Genome annotation databases

GeneID2540269.
GenomeReviewsGene locus ppi1 in contig CU329671_GR.
KEGGspo:SPBC28F2.03.
NMPDRfig|4896.1.peg.1530.

Organism-specific databases

GeneDB_SpombeSPBC28F2.03.

Phylogenomic databases

OMADVEADGQ.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003690-MON.
BRENDA5.2.1.8. 653.

Gene expression databases

ArrayExpressP18253.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCYPH_SCHPO
AccessionPrimary (citable) accession number: P18253
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 3, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents