Peptidylprolyl isomerase A

Peptidylprolyl isomerase A (cyclophilin A)
PDB rendering based on 1ak4.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AK4, 1AWQ, 1AWR, 1AWS, 1AWT, 1AWU, 1AWV, 1BCK, 1CWA, 1CWB, 1CWC, 1CWF, 1CWH, 1CWI, 1CWJ, 1CWK, 1CWL, 1CWM, 1CWO, 1FGL, 1M63, 1M9C, 1M9D, 1M9E, 1M9F, 1M9X, 1M9Y, 1MF8, 1MIK, 1NMK, 1OCA, 1RMH, 1VBS, 1VBT, 1W8L, 1W8M, 1W8V, 1YND, 1ZKF, 2ALF, 2CPL, 2CYH, 2RMA, 2RMB, 2X25, 2X2A, 2X2C, 2X2D, 2XGY, 3CYH, 3CYS, 3K0M, 3K0N, 3K0O, 3K0P, 3K0Q, 3K0R, 3ODI, 3ODL, 3RDD, 4CYH, 4IPZ, 5CYH
Identifiers
Symbols	PPIA ; CYPA; CYPH; HEL-S-69p
External IDs	OMIM: 123840 MGI: 3648545 HomoloGene: 134504 IUPHAR: 2751 ChEMBL: 1949 GeneCards: PPIA Gene
EC number	5.2.1.8
Gene ontology Molecular function • peptidyl-prolyl cis-trans isomerase activity • protein binding • peptide binding • poly(A) RNA binding • virion binding • unfolded protein binding Cellular component • extracellular region • extracellular space • nucleus • cytosol • membrane • extracellular vesicular exosome Biological process • protein peptidyl-prolyl isomerization • platelet degranulation • RNA-dependent DNA replication • protein folding • blood coagulation • viral process • viral life cycle • uncoating of virus • virion assembly • viral release from host cell • platelet activation • entry into host cell • lipid particle organization • regulation of viral genome replication • positive regulation of viral genome replication • positive regulation of protein secretion • leukocyte migration • establishment of integrated proviral latency Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5478	268373
Ensembl	ENSG00000196262	ENSMUSG00000062933
UniProt	P62937	P17742
RefSeq (mRNA)	NM_001300981	NM_008907
RefSeq (protein)	NP_001287910	NP_032933
Location (UCSC)	Chr 7: 44.84 – 44.86 Mb	Chr 11: 6.42 – 6.42 Mb
PubMed search

Peptidylprolyl isomerase A also known as cyclophilin A or rotamase A is an enzyme that in humans is encoded by the PPIA gene.^[1][2][3]

Function

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 accelerates 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.^[1]

Interactions

Peptidylprolyl isomerase A has been shown to interact with ITK.^[4]

See also

• Cyclophilin
• TRIM5alpha

References

Further reading

PDB gallery 1ak4: HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID  1awq: CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)  1awr: CYPA COMPLEXED WITH HAGPIA  1aws: SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)  1awt: SECYPA COMPLEXED WITH HAGPIA  1awu: CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER)  1awv: CYPA COMPLEXED WITH HVGPIA  1bck: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-THR CYCLOSPORIN  1cwa: X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION  1cwb: THE X-RAY STRUCTURE OF (MEBM2T)1-CYCLOSPORIN COMPLEXED WITH CYCLOPHILIN A PROVIDES AN EXPLANATION FOR ITS ANOMALOUSLY HIGH IMMUNOSUPPRESSIVE ACTIVITY  1cwc: IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN  1cwf: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN  1cwh: HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER CYCLOSPORIN  1cwi: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-(N-METHYL)-D-ALANINE CYCLOSPORIN  1cwj: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORIN  1cwk: HUMAN CYCLOPHILIN A COMPLEXED WITH 1-(6,7-DIHYDRO)MEBMT 2-VAL 3-D-(2-S-METHYL)SARCOSINE CYCLOSPORIN  1cwl: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 4-HYDROXY-MELEU CYCLOSPORIN  1cwm: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN  1cwo: HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN  1fgl: Cyclophilin A complexed with a fragment of HIV-1 GAG protein  1m63: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes  1m9c: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.  1m9d: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) O-type chimera Complex.  1m9e: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A Complex.  1m9f: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,A88M Complex.  1m9x: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,A88M,G89A Complex.  1m9y: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,G89A Complex.  1mf8: Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin  1mik: THE ROLE OF WATER MOLECULES IN THE STRUCTURE-BASED DESIGN OF (5-HYDROXYNORVALINE)-2-CYCLOSPORIN: SYNTHESIS, BIOLOGICAL ACTIVITY, AND CRYSTALLOGRAPHIC ANALYSIS WITH CYCLOPHILIN A  1nmk: The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-ray Crystal Structure and Binding Data  1oca: HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES  1rmh: RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL  1vbs: STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE  1vbt: Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF  1w8l: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES  1w8m: ENZYMATIC AND STRUCTURAL CHARACTERISATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES  1w8v: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES  1ynd: Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution  1zkf: Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA  2alf: crystal structure of human CypA mutant K131A  2cpl: SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION  2cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO  2rma: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A  2rmb: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A  3cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO  3cys: DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX  4cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE HIS-PRO  5cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO