PPIH_SCHPO
ID PPIH_SCHPO Reviewed; 173 AA.
AC O74729;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase cyp3;
DE Short=PPIase cyp3;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase cyp3;
GN Name=cyp3; ORFNames=SPBC1709.04c;
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 [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).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16134115; DOI=10.1002/yea.1288;
RA Pemberton T.J., Kay J.E.;
RT "The cyclophilin repertoire of the fission yeast Schizosaccharomyces
RT pombe.";
RL Yeast 22:927-945(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:16134115}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA21243.1; -; Genomic_DNA.
DR PIR; T39632; T39632.
DR RefSeq; NP_595437.1; NM_001021345.2.
DR AlphaFoldDB; O74729; -.
DR SMR; O74729; -.
DR BioGRID; 276731; 19.
DR STRING; 4896.SPBC1709.04c.1; -.
DR MaxQB; O74729; -.
DR PaxDb; O74729; -.
DR PRIDE; O74729; -.
DR EnsemblFungi; SPBC1709.04c.1; SPBC1709.04c.1:pep; SPBC1709.04c.
DR GeneID; 2540198; -.
DR KEGG; spo:SPBC1709.04c; -.
DR PomBase; SPBC1709.04c; cyp3.
DR VEuPathDB; FungiDB:SPBC1709.04c; -.
DR eggNOG; KOG0879; Eukaryota.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; O74729; -.
DR OMA; RHPNNPV; -.
DR PhylomeDB; O74729; -.
DR PRO; PR:O74729; -.
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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
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:0045292; P:mRNA cis splicing, via spliceosome; ISS: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; Cytoskeleton; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..173
FT /note="Peptidyl-prolyl cis-trans isomerase cyp3"
FT /id="PRO_0000232959"
FT DOMAIN 8..172
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 173 AA; 18906 MW; 116DA3AF5FED08B5 CRC64;
MSTEPVVFMD IAIDGRLLGR IKIRLFSSIV PKTAENFRQF CTGETLGVNQ KPIGYKNSTF
HRIIQGFMIQ GGDFVSGDGT GSATIFNSRT FPDENFTLKH DRPGLLSMAN AGKDSNGCQF
FITTVPCDFL DGKHVVFGEV IEGYDIVKEI ESTPVGANSR PKSNVAIVEC GEM
