CYPH_SCHPO
ID CYPH_SCHPO Reviewed; 162 AA.
AC P18253;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin;
DE Short=CPH;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase;
GN Name=ppi1; Synonyms=cyp2; ORFNames=SPBC28F2.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2204030; DOI=10.1093/nar/18.16.4917;
RA de Martin R., Philipson L.;
RT "The gene for cyclophilin (peptidyl-prolyl cis-trans isomerase) from
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 18:4917-4917(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K.,
RA Yanagida M.;
RT "S.pombe chromosome II cosmid 1228 sequence.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
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DR EMBL; X53223; CAA37322.1; -; Genomic_DNA.
DR EMBL; D83992; BAA12183.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB57932.1; -; Genomic_DNA.
DR PIR; S11212; CSZPA.
DR RefSeq; NP_595664.1; NM_001021559.2.
DR AlphaFoldDB; P18253; -.
DR SMR; P18253; -.
DR BioGRID; 276800; 5.
DR STRING; 4896.SPBC28F2.03.1; -.
DR iPTMnet; P18253; -.
DR MaxQB; P18253; -.
DR PaxDb; P18253; -.
DR PRIDE; P18253; -.
DR EnsemblFungi; SPBC28F2.03.1; SPBC28F2.03.1:pep; SPBC28F2.03.
DR GeneID; 2540269; -.
DR KEGG; spo:SPBC28F2.03; -.
DR PomBase; SPBC28F2.03; ppi1.
DR VEuPathDB; FungiDB:SPBC28F2.03; -.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; P18253; -.
DR OMA; SIVSMRV; -.
DR PhylomeDB; P18253; -.
DR PRO; PR:P18253; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:PomBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..162
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064130"
FT DOMAIN 5..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 162 AA; 17402 MW; B9F3747B7710C46E CRC64;
MSNCFFDVIA NGQPLGRIVF KLFDDVVPKT AANFRALCTG EKGYGYAGST FHRVIPQFML
QGGDFTRGNG TGGKSIYGEK FPDENFALKH NKPGLLSMAN AGPNTNGSQF FITTVVTPWL
DGKHVVFGEV TEGMDVVKKV ESLGSNSGAT RARIVIDKCG TV
