CYP7_SCHPO
ID CYP7_SCHPO Reviewed; 463 AA.
AC O42941;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Peptidylprolyl isomerase cyp7;
DE Short=PPIase cyp7;
DE EC=5.2.1.8;
DE AltName: Full=Complexed with cdc5 protein 27;
DE AltName: Full=Cyclophilin 7;
DE AltName: Full=Rotamase cyp7;
GN Name=cyp7; Synonyms=cwf27; ORFNames=SPBC16H5.05c;
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 IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. Catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Involved in pre-mRNA splicing.
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 -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA17903.1; -; Genomic_DNA.
DR PIR; T39621; T39621.
DR RefSeq; NP_595943.1; NM_001021851.2.
DR AlphaFoldDB; O42941; -.
DR SMR; O42941; -.
DR BioGRID; 276605; 38.
DR IntAct; O42941; 1.
DR STRING; 4896.SPBC16H5.05c.1; -.
DR iPTMnet; O42941; -.
DR MaxQB; O42941; -.
DR PaxDb; O42941; -.
DR EnsemblFungi; SPBC16H5.05c.1; SPBC16H5.05c.1:pep; SPBC16H5.05c.
DR PomBase; SPBC16H5.05c; cyp7.
DR VEuPathDB; FungiDB:SPBC16H5.05c; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_5_1; -.
DR InParanoid; O42941; -.
DR OMA; GTYGSQF; -.
DR PhylomeDB; O42941; -.
DR PRO; PR:O42941; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISO:PomBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISM:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 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 1: Evidence at protein level;
KW Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Rotamase; Spliceosome.
FT CHAIN 1..463
FT /note="Peptidylprolyl isomerase cyp7"
FT /id="PRO_0000064178"
FT DOMAIN 11..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 224..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 52174 MW; D7A3148A3CD74A83 CRC64;
MATLTNLEPL ATGTVILKTT RGDIQIELWC KEVPKACRNF IQLCLEGYYD GTIVHRVVPE
FLIQGGDPTG TGMGGESIYG EPFAVETHPR LRFIRRGLVG MACTENEGNN SQFFITLGPT
PEWNGKQTLF GRVVGDTIYN VVRISELELD ANQRPVFPPK IISTEVIDNY FTDIKPRSTK
EEREKIANEL AHQEKQKERN KLLKSGRRNK AVLSFGDEVD MPIVKKPLRQ KTPVSRSSDT
TTELSKDLIS SSSSIHSTYS SAQTGLTSAK VSSDEYARQV DTLDTKLNSS SKSKVQEEIS
RLKSELRDLE KSGGSSNSKP VVVRPKKRNI LTEELEKYKK SKKVVLGKRK NLENDEESTL
RALSSFQSKI RNAEDEDVMD SQYGSKIEDT PCSLHNVPGC FSCFDRLGEK NITETNSNWF
AHRLVAENDP TRRTEELRIQ RAEELKDVPS ARPKKLLMKR DII
