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P17742

- PPIA_MOUSE

UniProt

P17742 - PPIA_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

Ppia

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. protein peptidyl-prolyl isomerization Source: UniProtKB
    3. regulation of viral genome replication Source: UniProtKB

    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 region Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    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; alternate3 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.
    GenevestigatoriP17742.

    Interactioni

    Protein-protein interaction databases

    BioGridi234487. 4 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.
    OMAiHVERMVT.
    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

    MVNPTVFFDI TADDEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG    50
    SSFHRIIPGF MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM 100
    ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG 150
    KTSKKITISD CGQL 164
    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:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENSMUST00000071781; ENSMUSP00000071686; ENSMUSG00000062933.
    ENSMUST00000132846; ENSMUSP00000117987; ENSMUSG00000071866.
    GeneIDi268373.
    KEGGimmu:268373.
    UCSCiuc007hyn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS24419.1.
    PIRi S10327. CSMSA.
    RefSeqi NP_032933.1. NM_008907.1.
    UniGenei Mm.5246.

    3D structure databases

    ProteinModelPortali P17742.
    SMRi P17742. Positions 2-164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 234487. 4 interactions.
    IntActi P17742. 5 interactions.
    MINTi MINT-1856608.
    STRINGi 10090.ENSMUSP00000071686.

    PTM databases

    PhosphoSitei P17742.

    2D gel databases

    REPRODUCTION-2DPAGE P17742.
    SWISS-2DPAGE P17742.
    UCD-2DPAGE P17742.

    Proteomic databases

    MaxQBi P17742.
    PaxDbi P17742.
    PRIDEi P17742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000071781 ; ENSMUSP00000071686 ; ENSMUSG00000062933 .
    ENSMUST00000132846 ; ENSMUSP00000117987 ; ENSMUSG00000071866 .
    GeneIDi 268373.
    KEGGi mmu:268373.
    UCSCi uc007hyn.1. mouse.

    Organism-specific databases

    CTDi 5478.
    MGIi MGI:97749. Ppia.

    Phylogenomic databases

    eggNOGi COG0652.
    HOVERGENi HBG001065.
    InParanoidi P17742.
    KOi K03767.
    OMAi HVERMVT.
    OrthoDBi EOG79GT7W.
    TreeFami TF316719.

    Enzyme and pathway databases

    Reactomei REACT_211508. Basigin interactions.

    Miscellaneous databases

    NextBioi 392255.
    PROi P17742.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17742.
    CleanExi MM_PPIA.
    Genevestigatori P17742.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 153 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