CWC27_YEAST
ID CWC27_YEAST Reviewed; 301 AA.
AC Q02770; D6W3V1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Peptidyl-prolyl isomerase CWC27;
DE Short=PPIase CWC27;
DE EC=5.2.1.8;
DE AltName: Full=Complexed with CEF1 protein 27;
DE AltName: Full=Rotamase CWC27;
GN Name=CWC27; Synonyms=CYP7; OrderedLocusNames=YPL064C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION IN THE CWC COMPLEX, FUNCTION, AND IDENTIFICATION BY MASS
RP 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).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 (PubMed:11884590).
CC {ECO:0000250, ECO:0000269|PubMed:11884590}.
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 CWC complex (or CEF1-associated complex), a
CC spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at
CC least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21,
CC CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1,
CC MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46,
CC SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1,
CC SYF2, RSE1 and YJU2. {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC subfamily. {ECO:0000305}.
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DR EMBL; U39205; AAB68301.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11367.1; -; Genomic_DNA.
DR PIR; S60926; S60926.
DR RefSeq; NP_015261.1; NM_001183878.1.
DR PDB; 5GM6; EM; 3.50 A; b=1-301.
DR PDBsum; 5GM6; -.
DR AlphaFoldDB; Q02770; -.
DR SMR; Q02770; -.
DR BioGRID; 36115; 67.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-2778N; -.
DR IntAct; Q02770; 4.
DR MINT; Q02770; -.
DR STRING; 4932.YPL064C; -.
DR MaxQB; Q02770; -.
DR PaxDb; Q02770; -.
DR PRIDE; Q02770; -.
DR EnsemblFungi; YPL064C_mRNA; YPL064C; YPL064C.
DR GeneID; 856041; -.
DR KEGG; sce:YPL064C; -.
DR SGD; S000005985; CWC27.
DR VEuPathDB; FungiDB:YPL064C; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_0_1; -.
DR InParanoid; Q02770; -.
DR OMA; RNTWFIT; -.
DR BioCyc; YEAST:G3O-33973-MON; -.
DR PRO; PR:Q02770; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02770; protein.
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; IDA:SGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Rotamase; Spliceosome.
FT CHAIN 1..301
FT /note="Peptidyl-prolyl isomerase CWC27"
FT /id="PRO_0000064189"
FT DOMAIN 9..159
FT /note="PPIase cyclophilin-type"
FT REGION 251..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 35026 MW; 131A4138F6C993B8 CRC64;
MSSNIEPQTT AKCILYTTKG NIAIELWAKE CPETCKRFLS MLSDGTFTNG EFKELKPTQW
LMFNANSTGE YRTVAEEKNP RIRFNRDGLL GWDRRRNTWF ITVLADSKHV LNDCNVFGKI
VGKSIYIFRE ILGGEIEASS RDNDVKRFMY PAVLKDVEIT IPFFEDIFGS KRRLEDNEKK
EQEPAKKLVK SAKVKMVYED EQEDDDGDVQ KLKPRKRMIL PAWIKDDSRS EGIKLDASLD
QPQEALIREK TELHDNVDEA TTKETESQEN IKEEPMDKRE RETLAMLSKF QERIKNKNIL
K
