Q9FGC7 · ZEP_ARATH
- ProteinZeaxanthin epoxidase, chloroplastic
- GeneZEP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids667 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Zeaxanthin epoxidase that plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression and disease resistance and non-photochemical quencing (NPQ). Through its role in ABA biosynthesis, regulates the expression of stress-responsive genes such as RD29A during osmotic stress and is required for normal plant growth during vegetative development. Is required for late skotomorphogenic growth through its role in the xanthophyll carotenoids neoxanthin, violaxanthin and antheraxanthin biosynthesis. Required for beta-aminobutyric acid (BABA)-induced priming in disease resistance, tolerance to salt and drought stresses and sterility. Participates in NPQ by regulating the level of zeaxanthin in photosynthetic energy conversion. NPQ is a process that maintains the balance between dissipation and utilization of light energy to minimize the generation of oxidizing molecules and the molecular damages they can generate.
Miscellaneous
Plants overexpressing ZEP show increased levels of violaxanthin and ABA and increased tolerance to salt and drought stresses.
Catalytic activity
- all-trans-zeaxanthin + 4 reduced [2Fe-2S]-[ferredoxin] + 2 O2 + 4 H+ = all-trans-violaxanthin + 4 oxidized [2Fe-2S]-[ferredoxin] + 2 H2O
Cofactor
Pathway
Plant hormone biosynthesis; abscisate biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | membrane | |
Cellular Component | plastid | |
Molecular Function | FAD binding | |
Molecular Function | zeaxanthin epoxidase activity | |
Biological Process | abscisic acid biosynthetic process | |
Biological Process | response to heat | |
Biological Process | response to red light | |
Biological Process | response to water deprivation | |
Biological Process | sugar mediated signaling pathway | |
Biological Process | xanthophyll biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZeaxanthin epoxidase, chloroplastic
- EC number
- Short namesAtZEP
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FGC7
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Increased endogenous level of zeaxanthin and reduced level of ABA. Reduced size of leaves, inflorescences and flowers, early flowering, increased number of wilted plants, premature seed germination and reduced osmotic water permeability and ability to close stomata. Reduced susceptibility to virulent isolates of P.parasitica and sensitivity to BABA-induced priming.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 125 | In aba1-3; ABA-deficient phenotype. | ||||
Sequence: P → A | ||||||
Mutagenesis | 160 | In aba1-6; ABA-deficient phenotype. | ||||
Sequence: G → S | ||||||
Mutagenesis | 386 | In los6; reduces plant size, accelerates flowering and increases transpirational water loss. | ||||
Sequence: G → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-59 | Chloroplast | ||||
Sequence: MGSTPFCYSINPSPSKLDFTRTHVFSPVSKQFYLDLSSFSGKPGGVSGFRSRRALLGVK | ||||||
Chain | PRO_0000412072 | 60-667 | Zeaxanthin epoxidase, chloroplastic | |||
Sequence: AATALVEKEEKREAVTEKKKKSRVLVAGGGIGGLVFALAAKKKGFDVLVFEKDLSAIRGEGKYRGPIQIQSNALAALEAIDIEVAEQVMEAGCITGDRINGLVDGISGTWYVKFDTFTPAASRGLPVTRVISRMTLQQILARAVGEDVIRNESNVVDFEDSGDKVTVVLENGQRYEGDLLVGADGIWSKVRNNLFGRSEATYSGYTCYTGIADFIPADIESVGYRVFLGHKQYFVSSDVGGGKMQWYAFHEEPAGGADAPNGMKKRLFEIFDGWCDNVLDLLHATEEEAILRRDIYDRSPGFTWGKGRVTLLGDSIHAMQPNMGQGGCMAIEDSFQLALELDEAWKQSVETTTPVDVVSSLKRYEESRRLRVAIIHAMARMAAIMASTYKAYLGVGLGPLSFLTKFRVPHPGRVGGRFFVDIAMPSMLDWVLGGNSEKLQGRPPSCRLTDKADDRLREWFEDDDALERTIKGEWYLIPHGDDCCVSETLCLTKDEDQPCIVGSEPDQDFPGMRIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEGRRYRATPNFPARFRSSDIIEFGSDKKAAFRVKVIRKTPKSTRKNESNNDKLLQTA |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in leaves, stems and flowers, and at lower levels in roots and siliques.
Induction
By ABA and drought, salt and osmotic stresses.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 558-612 | FHA | ||||
Sequence: CIVGSEPDQDFPGMRIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEG |
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.
Q9FGC7-1
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
- Length667
- Mass (Da)73,842
- Last updated2001-03-01 v1
- Checksum89A0A6E6B8A26D5D
Q9FGC7-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 29 | in Ref. 3; AAG17703/AAG38877 | ||||
Sequence: S → A | ||||||
Sequence conflict | 42-54 | in Ref. 3; AAG17703/AAG38877 | ||||
Sequence: KPGGVSGFRSRRA → RSGGGLSVFRSRKT | ||||||
Sequence conflict | 76 | in Ref. 2; AAF82390/AAF82391 | ||||
Sequence: E → D | ||||||
Sequence conflict | 77 | in Ref. 3; AAG17703/AAG38877 | ||||
Sequence: Missing | ||||||
Sequence conflict | 116 | in Ref. 2; AAF82390/AAF82391 | ||||
Sequence: I → M | ||||||
Sequence conflict | 180-182 | in Ref. 2; AAF82390/AAF82391 | ||||
Sequence: ASR → GVT | ||||||
Sequence conflict | 194 | in Ref. 1; BAB11935 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_041638 | 581-610 | in isoform 2 | |||
Sequence: SKMHARVIYKDGAFFLMDLRSEHGTYVTDN → YKLYACSCDLQRRSFLLDGSSKRTRNLCDR | ||||||
Alternative sequence | VSP_041639 | 611-667 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB030296 EMBL· GenBank· DDBJ | BAB11935.1 EMBL· GenBank· DDBJ | mRNA | ||
AF134577 EMBL· GenBank· DDBJ | AAF82390.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF134578 EMBL· GenBank· DDBJ | AAF82391.1 EMBL· GenBank· DDBJ | mRNA | ||
AF281655 EMBL· GenBank· DDBJ | AAG17703.1 EMBL· GenBank· DDBJ | mRNA | ||
AF283761 EMBL· GenBank· DDBJ | AAG38877.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB026640 EMBL· GenBank· DDBJ | BAB08942.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED98292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED98293.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY081304 EMBL· GenBank· DDBJ | AAL91193.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AY093145 EMBL· GenBank· DDBJ | AAM13144.1 EMBL· GenBank· DDBJ | mRNA | ||
BT002560 EMBL· GenBank· DDBJ | AAO00920.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |