Q02770 (CWC27_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl isomerase CWC27
Short name=PPIase CWC27
EC=5.2.1.8

Alternative name(s):
Complexed with CEF1 protein 27
Rotamase CWC27

Gene names

Name:	CWC27
Synonyms:	CYP7
Ordered Locus Names:	YPL064C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Belongs to the CWC complex (or PRP19-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
Subcellular location	Cytoplasm. Nucleus Ref.4.
Miscellaneous	Present with 2360 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the cyclophilin-type PPIase family. CWC27 subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	U2-type spliceosomal complex Inferred from direct assay Ref.3. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Peptidyl-prolyl isomerase CWC27		PRO_0000064189
Regions
	Domain	9 – 159	151	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q02770 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 131A4138F6C993B8	FASTA	301	35,026
	10 20 30 40 50 60 MSSNIEPQTT AKCILYTTKG NIAIELWAKE CPETCKRFLS MLSDGTFTNG EFKELKPTQW 70 80 90 100 110 120 LMFNANSTGE YRTVAEEKNP RIRFNRDGLL GWDRRRNTWF ITVLADSKHV LNDCNVFGKI 130 140 150 160 170 180 VGKSIYIFRE ILGGEIEASS RDNDVKRFMY PAVLKDVEIT IPFFEDIFGS KRRLEDNEKK 190 200 210 220 230 240 EQEPAKKLVK SAKVKMVYED EQEDDDGDVQ KLKPRKRMIL PAWIKDDSRS EGIKLDASLD 250 260 270 280 290 300 QPQEALIREK TELHDNVDEA TTKETESQEN IKEEPMDKRE RETLAMLSKF QERIKNKNIL K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs." Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L. Mol. Cell. Biol. 22:2011-2024(2002) [PubMed: 11884590] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE CWC COMPLEX.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39205 Genomic DNA. Translation: AAB68301.1. BK006949 Genomic DNA. Translation: DAA11367.1.
PIR	S60926.
RefSeq	NP_015261.1. NM_001183878.1.
3D structure databases
ProteinModelPortal	Q02770.
SMR	Q02770. Positions 1-165.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2778N.
IntAct	Q02770. 3 interactions.
MINT	MINT-559936.
STRING	Q02770.
Proteomic databases
PeptideAtlas	Q02770.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL064C; YPL064C; YPL064C.
GeneID	856041.
KEGG	sce:YPL064C.
NMPDR	fig|4932.3.peg.6394.
Organism-specific databases
CYGD	YPL064c.
SGD	S000005985. CWC27.
Phylogenomic databases
eggNOG	fuNOG06026.
GeneTree	EFGT00050000000590.
OMA	IELWAKE.
OrthoDB	EOG4XD70H.
Gene expression databases
ArrayExpress	Q02770.
Genevestigator	Q02770.
GermOnline	YPL064C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K01802.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. False negative. PS50072. CSA_PPIASE_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	980983.

Entry information

Entry name

CWC27_YEAST

Accession

Primary (citable) accession number: Q02770
Secondary accession number(s): D6W3V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program