Q9SWS1 · ACFR2_ARATH
- ProteinTransmembrane ascorbate ferrireductase 2
- GeneCYB561B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids230 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Two-heme-containing cytochrome (PubMed:24449903).
Catalyzes ascorbate-dependent transmembrane ferric-chelate reduction (Probable)
Catalyzes ascorbate-dependent transmembrane ferric-chelate reduction (Probable)
Catalytic activity
- Fe3+(out) + L-ascorbate(in) = Fe2+(out) + H+ + monodehydro-L-ascorbate radical(in)Fe3+ (out)CHEBI:29034
+ L-ascorbate (in)CHEBI:38290= Fe2+ (out)CHEBI:29033+ CHEBI:15378 + CHEBI:59513
Cofactor
Note: Binds 2 heme b groups non-covalently.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 51 | Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 77 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 81 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 84 | Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 105 | monodehydro-L-ascorbate radical (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 106 | monodehydro-L-ascorbate radical (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 115 | monodehydro-L-ascorbate radical (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 118 | Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 140 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 150 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 151 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 157 | Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 182 | monodehydro-L-ascorbate radical (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 186 | monodehydro-L-ascorbate radical (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Molecular Function | ferric-chelate reductase activity | |
Molecular Function | metal ion binding | |
Molecular Function | transmembrane ascorbate ferrireductase activity | |
Biological Process | L-ascorbic acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransmembrane ascorbate ferrireductase 2
- EC number
- 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 accessionQ9SWS1
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 5-25 | Helical; Name=1 | ||||
Sequence: VLGGFPIFMVVRVLGFIIAAL | ||||||
Transmembrane | 50-70 | Helical; Name=2 | ||||
Sequence: VHPVMMVIGLILFNGEAMLAY | ||||||
Transmembrane | 82-102 | Helical; Name=3 | ||||
Sequence: LVHLTLQLTAFILSLIGVWAA | ||||||
Transmembrane | 120-140 | Helical; Name=4 | ||||
Sequence: WLGLACLFLFAFQWAAGFVTY | ||||||
Transmembrane | 157-177 | Helical; Name=5 | ||||
Sequence: HVFLGISIYALALVTATTGIL | ||||||
Transmembrane | 198-218 | Helical; Name=6 | ||||
Sequence: LVNTMGVLILILGGFVILGVV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 81 | Abrogates electron transfer; when associated with W-105/E-106/A-150. | ||||
Sequence: K → A | ||||||
Mutagenesis | 105 | Abrogates electron transfer; when associated with A-81/E-106/A-150. | ||||
Sequence: F → W | ||||||
Mutagenesis | 106 | Abrogates electron transfer; when associated with A-81/W-105/A-150. | ||||
Sequence: H → E | ||||||
Mutagenesis | 150 | Abrogates electron transfer; when associated with A-81/W-105/E-106. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412908 | 1-230 | Transmembrane ascorbate ferrireductase 2 | |||
Sequence: MAVPVLGGFPIFMVVRVLGFIIAALVLTWTVHYRGGLALSSDNKDHIFNVHPVMMVIGLILFNGEAMLAYKSVQGTKNLKKLVHLTLQLTAFILSLIGVWAALKFHIDKGIENFYSLHSWLGLACLFLFAFQWAAGFVTYWYPGGSRNSRASLMPWHVFLGISIYALALVTATTGILEKVTFLQVNQVITRYSTEAMLVNTMGVLILILGGFVILGVVTPVSGKDQVLTQ |
Proteomic databases
Expression
Tissue specificity
Expressed in roots, seedlings, leaves and flowers. Expressed in the L1 layer of the shoot apex, in the epidermis of leaf primordia and young leaves and in vascular bundles. In the differentiation zone of the root, detected in the pericycle and in the epidermis, but not in the cortex. Strongly expressed in the cortical region of the root tip, in the meristematic tissue and in the epidermal cell layer of lateral roots, but not in the root caps. Highly expressed in unfertilized ovules. In mature embryos, expressed in the epidermis, cotyledon tips and root tips.
Developmental stage
Strong reduction in expression levels in flowers following fertilization.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-218 | Cytochrome b561 | ||||
Sequence: VVRVLGFIIAALVLTWTVHYRGGLALSSDNKDHIFNVHPVMMVIGLILFNGEAMLAYKSVQGTKNLKKLVHLTLQLTAFILSLIGVWAALKFHIDKGIENFYSLHSWLGLACLFLFAFQWAAGFVTYWYPGGSRNSRASLMPWHVFLGISIYALALVTATTGILEKVTFLQVNQVITRYSTEAMLVNTMGVLILILGGFVILGVV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length230
- Mass (Da)25,289
- Last updated2000-05-01 v1
- Checksum544F69F682C9D259
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF132115 EMBL· GenBank· DDBJ | AAD45585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB049627 EMBL· GenBank· DDBJ | BAB21521.1 EMBL· GenBank· DDBJ | mRNA | ||
AB005231 EMBL· GenBank· DDBJ | BAB10153.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED94343.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT024611 EMBL· GenBank· DDBJ | ABD43009.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085028 EMBL· GenBank· DDBJ | AAM61586.1 EMBL· GenBank· DDBJ | mRNA | ||
AK117270 EMBL· GenBank· DDBJ | BAC41943.1 EMBL· GenBank· DDBJ | mRNA | ||
Z26702 EMBL· GenBank· DDBJ | CAA81401.1 EMBL· GenBank· DDBJ | mRNA |