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P17742 (PPIA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase A

Short name=PPIase A
EC=5.2.1.8
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
SP18
Gene names
Name:Ppia
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. 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.

Post-translational modification

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.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptidyl-prolyl cis-trans isomerase A
PRO_0000423245
Initiator methionine11Removed; alternate Ref.4 Ref.5 Ref.6
Chain2 – 164163Peptidyl-prolyl cis-trans isomerase A, N-terminally processed
PRO_0000064117

Regions

Domain7 – 163157PPIase cyclophilin-type

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed By similarity
Modified residue281N6-acetyllysine; alternate By similarity
Modified residue441N6-acetyllysine By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue931Phosphothreonine By similarity
Modified residue1251N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine By similarity
Modified residue1331N6-acetyllysine Ref.8
Glycosylation1081N-linked (GlcNAc...) Potential
Cross-link28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict13 – 142DD → NE in BAB27089. Ref.2
Sequence conflict18 – 203GRV → TXP AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P17742 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3528824224EA8849

FASTA16417,971
        10         20         30         40         50         60 
MVNPTVFFDI TADDEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SSFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE 

       130        140        150        160 
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITISD CGQL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS24419.1.
PIRCSMSA. S10327.
RefSeqNP_032933.1. NM_008907.1.
UniGeneMm.5246.

3D structure databases

ProteinModelPortalP17742.
SMRP17742. Positions 2-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234487. 4 interactions.
IntActP17742. 5 interactions.
MINTMINT-1856608.
STRING10090.ENSMUSP00000071686.

PTM databases

PhosphoSiteP17742.

2D gel databases

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

Proteomic databases

MaxQBP17742.
PaxDbP17742.
PRIDEP17742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071781; ENSMUSP00000071686; ENSMUSG00000062933.
ENSMUST00000132846; ENSMUSP00000117987; ENSMUSG00000071866.
GeneID268373.
KEGGmmu:268373.
UCSCuc007hyn.1. mouse.

Organism-specific databases

CTD5478.
MGIMGI:97749. Ppia.

Phylogenomic databases

eggNOGCOG0652.
HOVERGENHBG001065.
InParanoidP17742.
KOK03767.
OMAHVERMVT.
OrthoDBEOG79GT7W.
TreeFamTF316719.

Gene expression databases

BgeeP17742.
CleanExMM_PPIA.
GenevestigatorP17742.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio392255.
PROP17742.
SOURCESearch...

Entry information

Entry namePPIA_MOUSE
AccessionPrimary (citable) accession number: P17742
Secondary accession number(s): Q9CWJ5, Q9R137
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot