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Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Rotamase
Smp17.7
p17.7
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641271 – 161Peptidyl-prolyl cis-trans isomeraseAdd BLAST161

Proteomic databases

PRIDEiQ26565

Expressioni

Tissue specificityi

Found mainly in the tegument, gut epithelium, and muscle layers. Also found in the interior of the parasite.

Gene expression databases

ExpressionAtlasiQ26565 baseline

Structurei

3D structure databases

ProteinModelPortaliQ26565
SMRiQ26565
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 160PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST155

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0865 Eukaryota
COG0652 LUCA
HOGENOMiHOG000065981
KOiK09565
OMAiASQRPKV
OrthoDBiEOG091G0BGL
PhylomeDBiQ26565

Family and domain databases

Gene3Di2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
PANTHERiPTHR11071 PTHR11071, 1 hit
PfamiView protein in Pfam
PF00160 Pro_isomerase, 1 hit
PIRSFiPIRSF001467 Peptidylpro_ismrse, 1 hit
PRINTSiPR00153 CSAPPISMRASE
SUPFAMiSSF50891 SSF50891, 1 hit
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q26565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKAFFDIK AGDERLGRII FELFNDVPDT TRNFRELCTH KNNFGYKGSV
60 70 80 90 100
FHRIIPGFMC QGGDFTNGDG TGGKSIYGNK FKDENFNHKH EAFSLSMANA
110 120 130 140 150
GPNTNGSQFF ITTVPCSWLD GKHVVFGKVV SGIDVVKKME SLGSTSGKPS
160
KKIIIEDCGE C
Length:161
Mass (Da):17,671
Last modified:November 1, 1996 - v1
Checksum:iBB3D3C4EF874F527
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46884 mRNA Translation: AAB41257.1
RefSeqiXP_018652799.1, XM_018797792.1
UniGeneiSma.355

Genome annotation databases

EnsemblMetazoaiSmp_040130.1; Smp_040130.1:pep; Smp_040130
GeneDBiSmp_040130.1:pep
GeneIDi8347523
KEGGismm:Smp_040130

Similar proteinsi

Entry informationi

Entry nameiPPIA_SCHMA
AccessioniPrimary (citable) accession number: Q26565
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health