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P62940

- PPIA_MACMU

UniProt

P62940 - PPIA_MACMU

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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene
PPIA, CYPA
Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

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; alternate By 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-acetylmethionine By similarity
Modified residuei2 – 21N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed By similarity
Modified residuei28 – 281N6-acetyllysine; alternate By similarity
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei44 – 441N6-acetyllysine By similarity
Modified residuei76 – 761N6-acetyllysine By similarity
Modified residuei82 – 821N6-acetyllysine By similarity
Modified residuei93 – 931Phosphothreonine By similarity
Glycosylationi108 – 1081N-linked (GlcNAc...) Reviewed prediction
Modified residuei125 – 1251N6-acetyllysine By similarity
Modified residuei131 – 1311N6-acetyllysine By similarity
Modified residuei133 – 1331N6-acetyllysine By 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.

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.

Miscellaneous databases

EvolutionaryTraceiP62940.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 163157PPIase cyclophilin-typeAdd
BLAST

Sequence similaritiesi

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: June 11, 2014
This is version 83 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

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