Q26551 (PPIB_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Cyclophilin B
Rotamase B
S-cyclophilin

Gene names

Name:

CYP

Organism

Schistosoma mansoni (Blood fluke)

Taxonomic identifier

6183 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Inhibited by cyclosporin A (CsA).
Subcellular location	Endoplasmic reticulum lumen By similarity.
Developmental stage	This soluble protein is present in abundance in the adult worm as well as in the schistosomula and the eggs.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 213	190	Peptidyl-prolyl cis-trans isomerase B		PRO_0000025484
Regions
	Domain	35 – 197	163	PPIase cyclophilin-type
	Motif	210 – 213	4	Prevents secretion from ER By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q26551 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 15FF6371E60B7415	FASTA	213	23,294
	10 20 30 40 50 60 MAVLKPLCPL LLLSIICFGL IRSEANGPKV TDKVFFDIEV DGKPLARIII GLFGKTVPKT 70 80 90 100 110 120 VENFKQLSIG TQLKDGRTAS YKGSTFHRVI KSFMIQGGDF TNHDGTGGFS IYGDRFPDEN 130 140 150 160 170 180 FKLRHVGAGW LSMANAGPDT NGSQFFITTV KTSWLDGKHV VFGKVVEGMN IVRQIESETT 190 200 210 DSRDRPVKSI KIASCGHIPV EIPFSVTNSD AVE

References

[1]

"Characterization of a Schistosoma mansoni cDNA encoding a B-like cyclophilin and its expression in Escherichia coli." Klinkert M.-Q., Bugli F., Engels B., Carrasquillo E., Valle C., Cioli D. Mol. Biochem. Parasitol. 75:99-111(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Puerto Rican.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30874 mRNA. Translation: AAC46985.1.
3D structure databases
ProteinModelPortal	Q26551.
SMR	Q26551. Positions 27-206.
ModBase	Search...
Proteomic databases
PRIDE	Q26551.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HOG000065981.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
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

PPIB_SCHMA

Accession

Primary (citable) accession number: Q26551

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)