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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

Ppia

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  1. peptide binding Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  3. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. lipid particle organization Source: MGI
  2. neuron differentiation Source: MGI
  3. positive regulation of protein secretion Source: MGI
  4. positive regulation of viral genome replication Source: MGI
  5. protein folding Source: InterPro
  6. protein peptidyl-prolyl isomerization Source: UniProtKB
  7. regulation of viral genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

ReactomeiREACT_211508. Basigin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase A (EC:5.2.1.8)
Short name:
PPIase A
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
SP18
Cleaved into the following chain:
Gene namesi
Name:Ppia
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97749. Ppia.

Subcellular locationi

Cytoplasm. Secreted By similarity
Note: Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular space Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. focal adhesion Source: MGI
  5. membrane Source: MGI
  6. myelin sheath Source: UniProtKB
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptidyl-prolyl cis-trans isomerase APRO_0000423245Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity3 Publications
Chaini2 – 164163Peptidyl-prolyl cis-trans isomerase A, N-terminally processedPRO_0000064117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processedBy similarity
Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei44 – 441N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysineBy similarity
Modified residuei93 – 931PhosphothreonineBy similarity
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei133 – 1331N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17742.
PaxDbiP17742.
PRIDEiP17742.

2D gel databases

REPRODUCTION-2DPAGEP17742.
SWISS-2DPAGEP17742.
UCD-2DPAGEP17742.

PTM databases

PhosphoSiteiP17742.

Expressioni

Gene expression databases

BgeeiP17742.
CleanExiMM_PPIA.
ExpressionAtlasiP17742. baseline and differential.
GenevestigatoriP17742.

Interactioni

Subunit structurei

Interacts with PRPF19 isoform 2 (via N-terminus).1 Publication

Protein-protein interaction databases

BioGridi234487. 5 interactions.
IntActiP17742. 5 interactions.
MINTiMINT-1856608.
STRINGi10090.ENSMUSP00000071686.

Structurei

3D structure databases

ProteinModelPortaliP17742.
SMRiP17742. Positions 2-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 163157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
HOVERGENiHBG001065.
InParanoidiP17742.
KOiK03767.
OMAiFHRVMAG.
OrthoDBiEOG79GT7W.
TreeFamiTF316719.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNPTVFFDI TADDEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SSFHRIIPGF MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG
160
KTSKKITISD CGQL
Length:164
Mass (Da):17,971
Last modified:January 23, 2007 - v2
Checksum:i3528824224EA8849
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142DD → NE in BAB27089 (PubMed:16141072).Curated
Sequence conflicti18 – 203GRV → TXP AA sequence (PubMed:1565646).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52803 mRNA. Translation: CAA36989.1.
AK002236 mRNA. Translation: BAB21954.1.
AK007981 mRNA. Translation: BAB25387.1.
AK010649 mRNA. Translation: BAB27089.1.
AK012531 mRNA. Translation: BAB28300.1.
AK012663 mRNA. Translation: BAB28392.1.
AK028210 mRNA. Translation: BAC25817.1.
BC083076 mRNA. Translation: AAH83076.1.
AF171073 Genomic DNA. Translation: AAD50996.1.
CCDSiCCDS24419.1.
PIRiS10327. CSMSA.
RefSeqiNP_032933.1. NM_008907.1.
UniGeneiMm.5246.

Genome annotation databases

EnsembliENSMUST00000132846; ENSMUSP00000117987; ENSMUSG00000071866.
GeneIDi268373.
KEGGimmu:268373.
UCSCiuc007hyn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52803 mRNA. Translation: CAA36989.1.
AK002236 mRNA. Translation: BAB21954.1.
AK007981 mRNA. Translation: BAB25387.1.
AK010649 mRNA. Translation: BAB27089.1.
AK012531 mRNA. Translation: BAB28300.1.
AK012663 mRNA. Translation: BAB28392.1.
AK028210 mRNA. Translation: BAC25817.1.
BC083076 mRNA. Translation: AAH83076.1.
AF171073 Genomic DNA. Translation: AAD50996.1.
CCDSiCCDS24419.1.
PIRiS10327. CSMSA.
RefSeqiNP_032933.1. NM_008907.1.
UniGeneiMm.5246.

3D structure databases

ProteinModelPortaliP17742.
SMRiP17742. Positions 2-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234487. 5 interactions.
IntActiP17742. 5 interactions.
MINTiMINT-1856608.
STRINGi10090.ENSMUSP00000071686.

PTM databases

PhosphoSiteiP17742.

2D gel databases

REPRODUCTION-2DPAGEP17742.
SWISS-2DPAGEP17742.
UCD-2DPAGEP17742.

Proteomic databases

MaxQBiP17742.
PaxDbiP17742.
PRIDEiP17742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000132846; ENSMUSP00000117987; ENSMUSG00000071866.
GeneIDi268373.
KEGGimmu:268373.
UCSCiuc007hyn.1. mouse.

Organism-specific databases

CTDi5478.
MGIiMGI:97749. Ppia.

Phylogenomic databases

eggNOGiCOG0652.
HOVERGENiHBG001065.
InParanoidiP17742.
KOiK03767.
OMAiFHRVMAG.
OrthoDBiEOG79GT7W.
TreeFamiTF316719.

Enzyme and pathway databases

ReactomeiREACT_211508. Basigin interactions.

Miscellaneous databases

NextBioi392255.
PROiP17742.
SOURCEiSearch...

Gene expression databases

BgeeiP17742.
CleanExiMM_PPIA.
ExpressionAtlasiP17742. baseline and differential.
GenevestigatoriP17742.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA coding for mouse cyclophilin."
    Hasel K.W., Sutcliffe J.G.
    Nucleic Acids Res. 18:4019-4019(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Thymus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Embryonic stem cell, Kidney and Pancreas.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  4. "Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide-activated macrophages."
    Sherry B., Yarlett N., Strupp A., Cerami A.
    Proc. Natl. Acad. Sci. U.S.A. 89:3511-3515(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20; 22-28 AND 77-85.
    Tissue: Macrophage.
  5. "Cyclophilin-A is a zinc-dependent DNA binding protein in macrophages."
    Krummrei U., Bang R., Schmidtchen R., Brune K., Bang H.
    FEBS Lett. 371:47-51(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
    Tissue: Macrophage.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 56-59; 77-118; 132-144 AND 155-164, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  7. "Isolation, characterization and targeted disruption of mouse Ppia: cyclophilin A is not essential for mammalian cell viability."
    Colgan J., Asmal M., Luban J.
    Genomics 68:167-178(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-63.
    Strain: 129/Ola.
  8. "Involvement of the mouse Prp19 gene in neuronal/astroglial cell fate decisions."
    Urano Y., Iiduka M., Sugiyama A., Akiyama H., Uzawa K., Matsumoto G., Kawasaki Y., Tashiro F.
    J. Biol. Chem. 281:7498-7514(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRPF19.
    Strain: ICR.
    Tissue: Brain.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPPIA_MOUSE
AccessioniPrimary (citable) accession number: P17742
Secondary accession number(s): Q9CWJ5, Q9R137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.