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P62940

- PPIA_MACMU

UniProt

P62940 - PPIA_MACMU

Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

PPIA

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    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 By similarity.By similarity

    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

    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
    Cleaved into the following chain:
    Gene namesi
    Name:PPIA
    Synonyms:CYPA
    OrganismiMacaca mulatta (Rhesus macaque)
    Taxonomic identifieri9544 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
    ProteomesiUP000006718: Chromosome 3

    Subcellular locationi

    Cytoplasm By similarity. 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 – 165165Peptidyl-prolyl cis-trans isomerase APRO_0000064116Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 165164Peptidyl-prolyl cis-trans isomerase A, N-terminally processedPRO_0000423244Add
    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 residuei76 – 761N6-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-acetyllysineBy similarity

    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

    PRIDEiP62940.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48565N.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Beta strandi15 – 2410
    Turni26 – 283
    Helixi30 – 4112
    Turni42 – 443
    Beta strandi55 – 573
    Turni58 – 603
    Beta strandi61 – 644
    Beta strandi72 – 743
    Beta strandi97 – 1004
    Beta strandi102 – 1043
    Beta strandi112 – 1176
    Helixi120 – 1223
    Turni123 – 1253
    Beta strandi128 – 1325
    Helixi136 – 1438
    Beta strandi156 – 1638

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WLWX-ray1.50A1-165[»]
    4DGAX-ray1.90A/B1-165[»]
    4DGBX-ray1.70A1-165[»]
    4DGCX-ray2.65A/B/C/D/E1-165[»]
    4DGDX-ray1.40A1-165[»]
    4DGEX-ray2.20A/B1-165[»]
    ProteinModelPortaliP62940.
    SMRiP62940. Positions 2-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62940.

    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.
    GeneTreeiENSGT00750000117302.
    HOVERGENiHBG001065.
    InParanoidiP62940.
    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.

    P62940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG    50
    SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM 100
    ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG 150
    KTSKKITIAD CGQLE 165
    Length:165
    Mass (Da):18,012
    Last modified:January 23, 2007 - v2
    Checksum:i9B2E637A555E4434
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023861 mRNA. Translation: AAB81961.1.
    DQ251283 Genomic DNA. Translation: ABB77883.1.
    RefSeqiNP_001027981.1. NM_001032809.1.
    UniGeneiMmu.19758.

    Genome annotation databases

    EnsembliENSMMUT00000023383; ENSMMUP00000021879; ENSMMUG00000016638.
    GeneIDi574102.
    KEGGimcc:574102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023861 mRNA. Translation: AAB81961.1 .
    DQ251283 Genomic DNA. Translation: ABB77883.1 .
    RefSeqi NP_001027981.1. NM_001032809.1.
    UniGenei Mmu.19758.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WLW X-ray 1.50 A 1-165 [» ]
    4DGA X-ray 1.90 A/B 1-165 [» ]
    4DGB X-ray 1.70 A 1-165 [» ]
    4DGC X-ray 2.65 A/B/C/D/E 1-165 [» ]
    4DGD X-ray 1.40 A 1-165 [» ]
    4DGE X-ray 2.20 A/B 1-165 [» ]
    ProteinModelPortali P62940.
    SMRi P62940. Positions 2-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48565N.

    Chemistry

    BindingDBi P62940.

    Proteomic databases

    PRIDEi P62940.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMMUT00000023383 ; ENSMMUP00000021879 ; ENSMMUG00000016638 .
    GeneIDi 574102.
    KEGGi mcc:574102.

    Organism-specific databases

    CTDi 5478.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00750000117302.
    HOVERGENi HBG001065.
    InParanoidi P62940.
    KOi K03767.
    OMAi HVERMVT.
    OrthoDBi EOG79GT7W.
    TreeFami TF316719.

    Miscellaneous databases

    EvolutionaryTracei P62940.
    NextBioi 19968106.

    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. Luban J., Yin L.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Patterns of evolution of host proteins involved in retroviral pathogenesis."
      Ortiz M., Bleiber G., Martinez R., Kaessmann H., Telenti A.
      Retrovirology 3:11-11(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiPPIA_MACMU
    AccessioniPrimary (citable) accession number: P62940
    Secondary accession number(s): P05092
    , Q0ZQK4, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 84 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3