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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

Ppib

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.By similarity

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.Curated

Catalytic activityi

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

Enzyme regulationi

Inhibited by cyclosporin A (CsA).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-RNO-1650814 Collagen biosynthesis and modifying enzymes

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8By similarity)
Short name:
PPIase B
Alternative name(s):
CYP-S1
Cyclophilin B
Rotamase B
S-cyclophilin
Short name:
SCYLP
Gene namesi
Name:Ppib
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620312 Ppib

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33By similarityAdd BLAST33
ChainiPRO_000002548134 – 216Peptidyl-prolyl cis-trans isomerase BAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84N6-succinyllysineBy similarity1
Modified residuei165N6-acetyllysineBy similarity1
Modified residuei202S-nitrosocysteineBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, S-nitrosylation

Proteomic databases

PaxDbiP24368
PRIDEiP24368

PTM databases

iPTMnetiP24368
PhosphoSitePlusiP24368
SwissPalmiP24368

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney.1 Publication

Gene expression databases

BgeeiENSRNOG00000016781
GenevisibleiP24368 RN

Interactioni

Subunit structurei

Interacts with DYM. Interacts with CALR, CANX and CLGN (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Pdia4P386592EBI-916926,EBI-917435

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249051, 1 interactor
IntActiP24368, 4 interactors
MINTiP24368
STRINGi10116.ENSRNOP00000022828

Structurei

3D structure databases

SMRiP24368
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 204PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST158

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi213 – 216Prevents secretion from ERBy similarity4

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0880 Eukaryota
ENOG410Z0G4 LUCA
GeneTreeiENSGT00760000119072
HOGENOMiHOG000065981
HOVERGENiHBG001065
InParanoidiP24368
KOiK03768
OMAiEPFAVSK
OrthoDBiEOG091G0BGL
PhylomeDBiP24368
TreeFamiTF354259

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDF
60 70 80 90 100
QIGDEPVGRV TFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF
110 120 130 140 150
MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS
160 170 180 190 200
QFFITTVKTS WLDGKHVVFG KVLEGMDVVR KVENTKTDSR DKPLKDVIIV
210
DCGKIEVEKP FAIAKE
Length:216
Mass (Da):23,803
Last modified:November 25, 2008 - v3
Checksum:i8750D541754380D5
GO

Sequence cautioni

The sequence AAC25590 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54 – 70DEPVG…GKTVP → GRTCRTSDLWTLWKDCS (PubMed:2194066).CuratedAdd BLAST17
Sequence conflicti95 – 96RV → HM (PubMed:2194066).Curated2

Polymorphismi

Higher levels occur in the proximal convoluted tubule of strain SHR than strain Wistar Kyoto.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071225 mRNA Translation: AAC25590.1 Different initiation.
BC061971 mRNA Translation: AAH61971.1
PIRiS71547
RefSeqiNP_071981.1, NM_022536.2
UniGeneiRn.1893

Genome annotation databases

EnsembliENSRNOT00000022828; ENSRNOP00000022828; ENSRNOG00000016781
GeneIDi64367
KEGGirno:64367
UCSCiRGD:620312 rat

Similar proteinsi

Entry informationi

Entry nameiPPIB_RAT
AccessioniPrimary (citable) accession number: P24368
Secondary accession number(s): O88541
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 25, 2008
Last modified: June 20, 2018
This is version 138 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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