PIN1_SCHPO
ID PIN1_SCHPO Reviewed; 175 AA.
AC O74448;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase pin1;
DE Short=PPIase pin1;
DE EC=5.2.1.8;
GN Name=pin1; ORFNames=SPCC16C4.03;
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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11707530; DOI=10.1242/jcs.114.20.3779;
RA Huang H.-K., Forsburg S.L., John U.P., O'Connell M.J., Hunter T.;
RT "Isolation and characterization of the Pin1/Ess1p homologue in
RT Schizosaccharomyces pombe.";
RL J. Cell Sci. 114:3779-3788(2001).
CC -!- FUNCTION: Has a role in the G1/S stage transition of mitosis where it
CC is involved in the dephosphorylation of cdc25 and wee1.
CC {ECO:0000269|PubMed:11707530}.
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: Nucleus {ECO:0000269|PubMed:11707530}.
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DR EMBL; CU329672; CAA20742.1; -; Genomic_DNA.
DR PIR; T41093; T41093.
DR RefSeq; NP_587913.1; NM_001022904.2.
DR AlphaFoldDB; O74448; -.
DR SMR; O74448; -.
DR BioGRID; 275788; 4.
DR STRING; 4896.SPCC16C4.03.1; -.
DR iPTMnet; O74448; -.
DR MaxQB; O74448; -.
DR PaxDb; O74448; -.
DR PRIDE; O74448; -.
DR EnsemblFungi; SPCC16C4.03.1; SPCC16C4.03.1:pep; SPCC16C4.03.
DR GeneID; 2539218; -.
DR KEGG; spo:SPCC16C4.03; -.
DR PomBase; SPCC16C4.03; pin1.
DR VEuPathDB; FungiDB:SPCC16C4.03; -.
DR eggNOG; KOG3259; Eukaryota.
DR HOGENOM; CLU_090028_0_0_1; -.
DR InParanoid; O74448; -.
DR OMA; DEVQCLH; -.
DR PhylomeDB; O74448; -.
DR Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:O74448; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:PomBase.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:PomBase.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Cell cycle; Cell division; Isomerase; Mitosis; Nucleus; Reference proteome;
KW Rotamase.
FT CHAIN 1..175
FT /note="Peptidyl-prolyl cis-trans isomerase pin1"
FT /id="PRO_0000193443"
FT DOMAIN 4..38
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 64..175
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 175 AA; 19773 MW; ABA637835471BD25 CRC64;
MSNTGLPKPW IVKISRSRNR PYFFNTETHE SLWEPPAATD MAALKKFIAN ELQESVTPTE
ASNSPKIRAS HLLVKHRESR RPSSWKEEHI TRSKEEARKL AEHYEQLLKS GSVSMHDLAM
KESDCSSARR GGELGEFGRD EMQKPFEDAA FALKPGEISG VVETSSGFHI IQRHA
