Q6Q152 · CPY57_ARATH
- ProteinPeptidyl-prolyl cis-trans isomerase CYP57
- GeneCYP57
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids504 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Involved in plant response to pathogen infection by increasing PAD4 expression in absence of EDS1 up-regulation
Involved in plant response to pathogen infection by increasing PAD4 expression in absence of EDS1 up-regulation
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasmodesma | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | protein folding |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase CYP57
- EC number
- Short namesPPIase CYP57
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ6Q152
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Disruption phenotype
Increased susceptibility to P.syringae infection.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 34 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000429942 | 2-504 | Peptidyl-prolyl cis-trans isomerase CYP57 | |||
Sequence: STVYVLEPPTKGKVIVNTTHGPIDVELWPKEAPKSVRNFVQLCLEGYFDNTIFHRVIPGFLVQGGDPTGSGTGGDSIYGGVFADEFHSRLRFSHRGIVAMANASSPNSNGSQFFFTLDKCDWLDKKHTIFGKVTGDSIYNLLRLGEVDTSKDDRPLDPAPKILSVEVLWNPFEDIVPRVLAKTSEESAAEIKEPPTKPVKKLNLLSFGEEAEEEEKELAVVKQKIKSSHDVLNDPRLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDKSFSVSDTVGNSDDDDDGEDETKFDAKMRNQVLSRRKEIGDTPSKPTQKKKSSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDTDLQLYNASERARQLHKLKKRRLQGNEDSVLAKLEKFKQSISAKPFTSSNEPVVLTSSSEPVDNKEEDLSDWKNVKLKFAPERGKDKMSRRDDPDAYMVVDPLLEKGKEKFNRMQAKQKRREREWSGKSLA |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Induction
Up-regulated upon pathogen infection.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-167 | PPIase cyclophilin-type | ||||
Sequence: IVNTTHGPIDVELWPKEAPKSVRNFVQLCLEGYFDNTIFHRVIPGFLVQGGDPTGSGTGGDSIYGGVFADEFHSRLRFSHRGIVAMANASSPNSNGSQFFFTLDKCDWLDKKHTIFGKVTGDSIYNLLRLGEVDTSKDDRPLDPAPKILSVE | ||||||
Coiled coil | 204-274 | |||||
Sequence: NLLSFGEEAEEEEKELAVVKQKIKSSHDVLNDPRLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDK | ||||||
Compositional bias | 237-274 | Basic and acidic residues | ||||
Sequence: RLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDK | ||||||
Region | 237-374 | Disordered | ||||
Sequence: RLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDKSFSVSDTVGNSDDDDDGEDETKFDAKMRNQVLSRRKEIGDTPSKPTQKKKSSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDT | ||||||
Compositional bias | 295-318 | Basic and acidic residues | ||||
Sequence: TKFDAKMRNQVLSRRKEIGDTPSK | ||||||
Compositional bias | 325-374 | Basic and acidic residues | ||||
Sequence: SSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDT | ||||||
Compositional bias | 416-433 | Polar residues | ||||
Sequence: AKPFTSSNEPVVLTSSSE | ||||||
Region | 416-441 | Disordered | ||||
Sequence: AKPFTSSNEPVVLTSSSEPVDNKEED | ||||||
Region | 482-504 | Disordered | ||||
Sequence: EKFNRMQAKQKRREREWSGKSLA |
Sequence similarities
Belongs to the cyclophilin-type PPIase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6Q152-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length504
- Mass (Da)56,515
- Last updated2004-07-05 v1
- Checksum824E62DA59EB113B
Q6Q152-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 59 | in Ref. 5; BAE99301 | ||||
Sequence: P → H | ||||||
Compositional bias | 237-274 | Basic and acidic residues | ||||
Sequence: RLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDK | ||||||
Alternative sequence | VSP_055393 | 249-252 | in isoform 2 | |||
Sequence: NASE → AKLY | ||||||
Alternative sequence | VSP_055394 | 253-504 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 295-318 | Basic and acidic residues | ||||
Sequence: TKFDAKMRNQVLSRRKEIGDTPSK | ||||||
Compositional bias | 325-374 | Basic and acidic residues | ||||
Sequence: SSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDT | ||||||
Compositional bias | 416-433 | Polar residues | ||||
Sequence: AKPFTSSNEPVVLTSSSE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY568525 EMBL· GenBank· DDBJ | AAS75308.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031804 EMBL· GenBank· DDBJ | CAA21215.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161582 EMBL· GenBank· DDBJ | CAB80023.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE86168.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT025329 EMBL· GenBank· DDBJ | ABF57285.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227277 EMBL· GenBank· DDBJ | BAE99301.1 EMBL· GenBank· DDBJ | mRNA |