Q94A16 · CP21C_ARATH
- ProteinPeptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial
- GeneCYP21-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids230 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase (By similarity).
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 | Golgi apparatus | |
Cellular Component | Golgi cis cisterna | |
Cellular Component | mitochondrion | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial
- EC number
- Short namesPPIase CYP21-3
- 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 accessionQ94A16
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, transit peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000044628 | ?-230 | Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial | |||
Sequence: MAKIKPQALLQQSKKKKGPSRISITNIVIYTLAVLLLVFVLFSAYRRWTHRSEIPTHNGRSVLEDAAFPGMKNVDLPRFATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKNIDTSLKHEEFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTLLQDM | ||||||
Transit peptide | 1-? | Mitochondrion |
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous, mostly in aerial organs.
Induction
Repressed by the munition hexahydro-1,3,5-trinitro-1,3,5-triazine, also known as Royal Demolition eXplosive (RDX).
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 76-226 | PPIase cyclophilin-type | ||||
Sequence: LPRFATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKNIDTSLKHEEFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTL |
Sequence similarities
Belongs to the cyclophilin-type PPIase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q94A16-1
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
- Length230
- Mass (Da)26,042
- Last updated2005-12-20 v2
- Checksum6198D43EE5B9552F
Q94A16-2
- Name2
- Differences from canonical
- 1-70: Missing
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055389 | 1-70 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY568520 EMBL· GenBank· DDBJ | AAS75303.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002337 EMBL· GenBank· DDBJ | AAB63832.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC10827.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY050450 EMBL· GenBank· DDBJ | AAK91465.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY097351 EMBL· GenBank· DDBJ | AAM19867.1 EMBL· GenBank· DDBJ | mRNA | ||
AK318997 EMBL· GenBank· DDBJ | BAH57112.1 EMBL· GenBank· DDBJ | mRNA |