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P62940 (PPIA_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:PPIA
Synonyms:CYPA
OrganismMacaca mulatta (Rhesus macaque) [Reference proteome]
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length165 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 By similarity.

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 By similarity.

Subcellular location

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.

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

Initiator methionine11Removed By similarity
Chain2 – 165164Peptidyl-prolyl cis-trans isomerase A
PRO_0000064116

Regions

Domain7 – 163157PPIase cyclophilin-type

Amino acid modifications

Modified residue21N-acetylvaline By similarity
Modified residue211Phosphoserine By similarity
Modified residue281N6-acetyllysine By similarity
Modified residue441N6-acetyllysine By similarity
Modified residue761N6-acetyllysine By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue931Phosphothreonine By similarity
Modified residue1251N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine By similarity
Glycosylation1081N-linked (GlcNAc...) Potential
Cross-link28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1 ............................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62940 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B2E637A555E4434

FASTA16518,012
        10         20         30         40         50         60 
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF 

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

       130        140        150        160 
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE

« Hide

References

[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF023861 mRNA. Translation: AAB81961.1.
DQ251283 Genomic DNA. Translation: ABB77883.1.
RefSeqNP_001027981.1. NM_001032809.1.
UniGeneMmu.19758.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP62940.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48565N.

Proteomic databases

PRIDEP62940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMMUT00000023383; ENSMMUP00000021879; ENSMMUG00000016638.
GeneID574102.
KEGGmcc:574102.

Organism-specific databases

CTD5478.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00690000101651.
HOVERGENHBG001065.
InParanoidP62940.
KOK03767.
OMAFIMHKNS.
OrthoDBEOG4DJJXN.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP62940.
EvolutionaryTraceP62940.
NextBio19968106.

Entry information

Entry namePPIA_MACMU
AccessionPrimary (citable) accession number: P62940
Secondary accession number(s): P05092 expand/collapse secondary AC list , Q0ZQK4, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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