P18253 (CYPH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Cyclophilin
Short name=CPH
Cyclosporin A-binding protein
Rotamase

Gene names

Name:	ppi1
Synonyms:	cyp2
ORF Names:	SPBC28F2.03

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	162 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 162	162	Peptidyl-prolyl cis-trans isomerase		PRO_0000064130
Regions
	Domain	5 – 161	157	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P18253 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: B9F3747B7710C46E	FASTA	162	17,402
	10 20 30 40 50 60 MSNCFFDVIA NGQPLGRIVF KLFDDVVPKT AANFRALCTG EKGYGYAGST FHRVIPQFML 70 80 90 100 110 120 QGGDFTRGNG TGGKSIYGEK FPDENFALKH NKPGLLSMAN AGPNTNGSQF FITTVVTPWL 130 140 150 160 DGKHVVFGEV TEGMDVVKKV ESLGSNSGAT RARIVIDKCG TV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene for cyclophilin (peptidyl-prolyl cis-trans isomerase) from Schizosaccharomyces pombe." de Martin R., Philipson L. Nucleic Acids Res. 18:4917-4917(1990) [PubMed: 2204030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"S.pombe chromosome II cosmid 1228 sequence." Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K., Yanagida M. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53223 Genomic DNA. Translation: CAA37322.1.
D83992 Genomic DNA. Translation: BAA12183.1.
CU329671 Genomic DNA. Translation: CAB57932.1.

PIR

CSZPA. S11212.

RefSeq

NP_595664.1. NM_001021559.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WVS	model	-	A	1-162	[»]

ProteinModelPortal

P18253.

SMR

P18253. Positions 1-160.

ModBase

Search...

Protein-protein interaction databases

STRING

P18253.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

SPBC28F2.03.1; SPBC28F2.03.1:pep; SPBC28F2.03.

GeneID

2540269.

GenomeReviews

Gene locus ppi1 in contig CU329671_GR.

KEGG

spo:SPBC28F2.03.

NMPDR

fig|4896.1.peg.1530.

Organism-specific databases

GeneDB_Spombe

SPBC28F2.03.

Phylogenomic databases

eggNOG

fuNOG08891.

GeneTree

EFGT00050000000590.

HOGENOM

HBG610621.

OMA

ARIVIAK.

OrthoDB

EOG4DZ54P.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-003690-MONOMER.

Gene expression databases

ArrayExpress

P18253.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

KO

K01802.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CYPH_SCHPO

Accession

Primary (citable) accession number: P18253

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program