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    PPIA peptidylprolyl isomerase A [ Homo sapiens (human) ]

    Gene ID: 5478, updated on 7-Feb-2016
    Official Symbol
    PPIAprovided by HGNC
    Official Full Name
    peptidylprolyl isomerase Aprovided by HGNC
    Primary source
    HGNC:HGNC:9253
    See related
    Ensembl:ENSG00000196262; HPRD:00457; HPRD:17376; MIM:123840; Vega:OTTHUMG00000023687
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    CYPA; CYPH; HEL-S-69p
    Summary
    This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported. [provided by RefSeq, Jul 2008]
    Orthologs
    See PPIA in Epigenomics, MapViewer
    Location:
    7p13
    Exon count:
    6
    Annotation release Status Assembly Chr Location
    107 current GRCh38.p2 (GCF_000001405.28) 7 NC_000007.14 (44796636..44803123)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 7 NC_000007.13 (44836241..44842716)

    Chromosome 7 - NC_000007.14Genomic Context describing neighboring genes Neighboring gene zinc finger, MIZ-type containing 2 Neighboring gene uncharacterized LOC105375259 Neighboring gene uncharacterized LOC105375260 Neighboring gene H2A histone family member V

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 env The interaction between exposed cyclophilin A (CypA) and cell surface heparans represents the initial step of HIV-1 attachment and is a necessary step for HIV-1 gp120 binding to CD4 PubMed
    env Macrophage- and T-cell-tropic V3 loop peptides of HIV-1 gp120 bind specifically to the active site of the immunophilins FK506-binding protein (FKBP12), and cyclophilins A and B, and inhibit their peptidyl-prolyl cis-trans isomerase (PPIase) activities PubMed
    Nef nef HIV-1 Nef downregulates the expression of cyclophilin A protein in Nef-transfected SupT1 cells PubMed
    nef Cyclophilin A has been demonstrated to bind to HIV-1 Nef using a biochemical binding assay, however the biological significance of this interaction is currently not known PubMed
    Pr55(Gag) gag Treatment of cells with cyclosporine A blocks the interaction of HIV-1 Gag with eEF2, indicating that cyclophilin A (CypA) stabilizes the Gag-eEF2 association PubMed
    gag Targeting of the catalytic HECT domain (residues 598-952) of NEDD4-2s to HIV-1 Gag via CypA is sufficient to rescue HIV-1 budding defects PubMed
    gag H219Q and H219P substitutions in the viral CypA binding loop of HIV-1 Gag reduces CypA incorporation into HIV-1 and potentiates viral replication in CypA-rich MT-2 and H9 cells PubMed
    gag A fusion protein CypA-Nef consisting of cyclophilin A (CypA) linked to the amino terminus of Nef enhances the infectivity of Nef-defective HIV-1 particles and is incorporated into virions via association with Gag during particle assembly PubMed
    gag Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association PubMed
    gag Cyclophilin A modulates processing of HIV-1 Gag by the viral protease PubMed
    Vif vif Vif has been demonstrated to bind to cyclophilin A using a biochemical binding assay PubMed
    Vpr vpr The complete C-terminal peptide Vpr75-90, comprising the 16 residues 75GCRHSRIGVTRQRRAR90, is required for maintaining the strong interaction with CypA in a 1:1 binding model. Replacement of R80 with alanine significantly reduces the binding affinity PubMed
    vpr Cyclophilin A catalyzes the prolyl cis/trans interconversion of proline residues at positions 5, 10, 14, and 35 in HIV-1 Vpr PubMed
    vpr Cyclophilin A interacts directly with HIV-1 Vpr to mediate the cis/trans-proline isomerization of Vpr, which is important for Vpr synthesis and function PubMed
    capsid gag HIV-1 N74D CA mutant has less binding affinity to CypA and less HIV-1 infectivity than wild type PubMed
    gag V86M capsid mutant, a single amino acid change in the cyclophilin-binding loop of the HIV-1 capsid protein, can replicate in cells expressing TRIM5alpha(rh). This involves decreased binding to TRIM5alpha(rh) and retention of binding to cyclophilin A PubMed
    gag Substitution of Thr for Ala at position 105 of CA (A105T) rescues the impaired single-cycle infectivity of T54A and A92E mutants, indicating that CA determinants outside the CypA-binding loop can modulate the dependence of HIV-1 infection on CypA PubMed
    gag The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells PubMed
    gag Binding of HIV-1 Capsid to cyclophilin A requires HIV-1 Gag dimerization PubMed
    gag Proline-90 and Glycine-89 of HIV-1 Capsid are required for the binding of cyclophilin A to Capsid PubMed
    gag HIV-1 Capsid and Gag proteins bind to cyclophilin A, resulting in the incorporation of cyclophilin A into virions, which is important for the completion of early steps in HIV-1 replication following entry of the virus into cells PubMed
    gag HIV-1 CA mutants N74D and P90A fail to bind to CPSF6 and cyclophilins (Nup358 and CypA), respectively, and trigger innate sensors, leading to nuclear translocation of NFkappaB and IRF3, production of type 1 IFN and induction of an antiviral state PubMed
    gag Cyclophilin A inhibits HIV-1 nuclear entry by promoting HIV-1 CA core stability PubMed
    gag The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolate-dependent, which can result in inhibition, no change, or an increase in viral infectivity PubMed
    gag Cyclophilin A stabilizes the HIV-1 CA and antagonizes TNPO3 acceleration of uncoating in vitro PubMed
    gag Inhibition of the HIV-1 CA-CypA interaction rescues the infectivity of CA-N121K HIV-1. The N121K mutant is inhibited by CypA in HIV-1 infected cells PubMed
    gag Cyclophilin A mutants, R55K, R55A, F113W, and H126A, exhibit the most pronounced decrease in PPIase activity compared to wild type. These mutants bind to HIV-1 CA with low affinity PubMed
    gag A small molecule HIV-1 inhibitor PF74 destabilizes the viral capsid in vitro and its antiviral activity is promoted by binding of the host protein cyclophilin A to the HIV-1 capsid PubMed
    gag Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts PubMed
    gag Delaying reverse transcription leads to a time-dependent loss in viral infectivity that is increased by inhibiting capsid-cyclophilin A interactions, but does not result in increased viral sensitivity to hTRIM5alpha PubMed
    gag CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway PubMed
    gag Cyclophilin A is acetylated at amino acid residue Lys125 in human cells. Acetylated cyclophilin A inhibits its catalysis, inhibits cyclosporine binding, and alters HIV-1 capsid interaction PubMed
    gag TRIM5 alpha-mediated resistance to HIV-1 in Old World monkey cells is modulated by the HIV-1 Capsid and cyclophilin A interaction PubMed
    gag The interaction between cyclophilin A and HIV-1 CA is required for the enhanced restriction of HIV-1 due to rhTRIM5alpha in non-dividing cells PubMed
    gag Alignment of primate lentiviral capsid protein sequences demonstrates that they have conserved the proline rich cyclophilin A binding loop on their outer surface PubMed
    gag Reducing the binding of CypA to the A92E mutant capsid, either by cyclosporine treatment or by an additional P90A change in the CA protein, increases the amount of particulate capsids and viral infectivity in HeLa cells PubMed
    gag H219Q and H219P substitutions in the cyclophilin A binding loop of HIV-1 CA enhance HIV-1 replication by reducing viral cyclophilin A content in resulting virions as produced in cyclophilin A-rich cells PubMed
    gag HIV-1 CA R264K mutant is impaired in generating late reverse transcription products, is inhibited by the presence of normal levels of cyclophilin A, and is rescued with the development of a rare secondary mutation S173A PubMed
    gag Increasing CypA levels in permissive TE671 cells restrict HIV-1 CA mutants A92E and G94D in a CypA-dependent way PubMed
    gag Cyclophilin A binding to HIV-1 Capsid modulates the sensitivity of HIV-1 to host restriction factors PubMed
    gag Cyclophilin A decreases the degree of capsid protein processing by the HIV-1 protease PubMed
    gag The HIV-1 p2 peptide (spacer peptide in the HIV-1 Gag polyprotein between Capsid and Nucleocapsid; SP1) is involved in the interaction between HIV-1 Capsid and cyclophilin A PubMed
    gag Cyclophilin A catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond of HIV-1 Capsid PubMed
    gag Cyclophilin A has a higher affinity for HIV-1 Gag than for the mature HIV-1 Capsid protein, as a result of additional interactions with the 12 C-terminal amino acids of HIV-1 Matrix PubMed
    gag The interaction of HIV-1 Capsid to cyclophilin A can be inhibited by cyclosporin A leading to inhibition of virus replication PubMed
    gag The active site hydrophobic binding pocket of cyclophilin A (amino acids 54-126) binds to the N-Terminal and central portion of HIV-1 Capsid, most importantly to Capsid amino acids 85-93 PubMed
    integrase gag-pol Compared to the HIV-1 IN wild type, two IN mutants (DeltaIN and C130S) have reduced levels of the cytoplasmic CA, suggesting accelerated uncoating. Virus derived from the IN mutants incorporates decreased levels of cyclophilin A (CypA) PubMed
    matrix gag The 12 carboxy-terminal amino acids of HIV-1 Matrix (p17; amino acids 121-132) are important for optimal binding of cyclophilin to HIV-1 Gag and Capsid (p24) PubMed
    gag Cyclophilin A binds to HIV-1 Matrix PubMed
    nucleocapsid gag Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts PubMed
    gag Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association PubMed
    p6 gag HIV-1 p6 binds to cyclophilin A, particularly, through the p6 proline residues, located at positions 5, 7, 10, 11, 24, 30, 37 and 49 PubMed
    retropepsin gag-pol Positional proteomics analysis identifies the cleavage of human peptidylprolyl isomerase A (PPIA; cyclophilin A) at amino acid residues 6-9 and 23-24 by the HIV-1 protease PubMed
    reverse transcriptase gag-pol The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells PubMed

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    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Clone Names

    • MGC12404, MGC23397, MGC117158

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    peptide binding IEA
    Inferred from Electronic Annotation
    more info
     
    peptidyl-prolyl cis-trans isomerase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    poly(A) RNA binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    unfolded protein binding TAS
    Traceable Author Statement
    more info
    PubMed 
    virion binding NAS
    Non-traceable Author Statement
    more info
    PubMed 
    Process Evidence Code Pubs
    RNA-dependent DNA replication TAS
    Traceable Author Statement
    more info
     
    blood coagulation TAS
    Traceable Author Statement
    more info
     
    entry into host cell TAS
    Traceable Author Statement
    more info
     
    establishment of integrated proviral latency TAS
    Traceable Author Statement
    more info
     
    leukocyte migration TAS
    Traceable Author Statement
    more info
     
    lipid particle organization IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    platelet activation TAS
    Traceable Author Statement
    more info
     
    platelet degranulation TAS
    Traceable Author Statement
    more info
     
    positive regulation of protein secretion IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    positive regulation of viral genome replication IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    protein folding TAS
    Traceable Author Statement
    more info
    PubMed 
    protein peptidyl-prolyl isomerization IDA
    Inferred from Direct Assay
    more info
    PubMed 
    regulation of viral genome replication IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    regulation of viral genome replication TAS
    Traceable Author Statement
    more info
    PubMed 
    uncoating of virus TAS
    Traceable Author Statement
    more info
     
    viral life cycle TAS
    Traceable Author Statement
    more info
     
    viral process TAS
    Traceable Author Statement
    more info
     
    viral release from host cell TAS
    Traceable Author Statement
    more info
    PubMed 
    virion assembly TAS
    Traceable Author Statement
    more info
     
    Component Evidence Code Pubs
    cytosol IDA
    Inferred from Direct Assay
    more info
    PubMed 
    cytosol TAS
    Traceable Author Statement
    more info
     
    extracellular exosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    extracellular region TAS
    Traceable Author Statement
    more info
     
    extracellular space IDA
    Inferred from Direct Assay
    more info
    PubMed 
    focal adhesion IDA
    Inferred from Direct Assay
    more info
    PubMed 
    membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nucleus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Preferred Names
    peptidyl-prolyl cis-trans isomerase A
    Names
    PPIase A
    T cell cyclophilin
    cyclosporin A-binding protein
    epididymis secretory sperm binding protein Li 69p
    peptidylprolyl isomerase A (cyclophilin A)
    rotamase A
    NP_001287910.1
    NP_066953.1

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_029697.1 RefSeqGene

      Range
      4995..11482
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001300981.1NP_001287910.1  peptidyl-prolyl cis-trans isomerase A isoform 2

      See identical proteins and their annotated locations for NP_001287910.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in its 5' UTR and uses a downstream start codon, compared to variant 1. The encoded isoform (2) has a shorter N-terminus, compared to isoform 1.
      Source sequence(s)
      AC013436, AK293003, BC137057
      Consensus CDS
      CCDS75592.1
      UniProtKB/Swiss-Prot
      P62937
      Conserved Domains (1) summary
      cl00197
      Location:1102
      cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...
    2. NM_021130.4NP_066953.1  peptidyl-prolyl cis-trans isomerase A isoform 1

      See identical proteins and their annotated locations for NP_066953.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the shorter transcript but encodes the longer isoform (1).
      Source sequence(s)
      AC013436, BC137057
      Consensus CDS
      CCDS5494.1
      UniProtKB/Swiss-Prot
      P62937
      UniProtKB/TrEMBL
      V9HWF5
      Related
      ENSP00000419425, OTTHUMP00000159501, ENST00000468812, OTTHUMT00000251293
      Conserved Domains (1) summary
      cd01926
      Location:4162
      cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p2 Primary Assembly

    Genomic

    1. NC_000007.14 Reference GRCh38.p2 Primary Assembly

      Range
      44796636..44803123
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate CHM1_1.1

    Genomic

    1. NC_018918.2 Alternate CHM1_1.1

      Range
      44840580..44847075
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Suppressed Reference Sequence(s)

    The following Reference Sequences have been suppressed. Explain

    1. NM_203430.1: Suppressed sequence

      Description
      NM_203430.1: This RefSeq was permanently suppressed because it uses an internal initiation methionine, which when corrected results in a nonsense-mediated mRNA decay (NMD) candidate.
    2. NM_203431.1: Suppressed sequence

      Description
      NM_203431.1: This RefSeq was permanently suppressed because it uses an internal initiation methionine, which when corrected results in a nonsense-mediated mRNA decay (NMD) candidate.