| IED ID | IndEnz0002001972 |
| Enzyme Type ID | protease001972 |
| Protein Name |
Transmembrane reductase CYB561D2 EC 7.2.1.3 Cytochrome b561 domain-containing protein 2 Putative tumor suppressor protein 101F6 |
| Gene Name | CYB561D2 101F6 LUCA12.2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MALSAETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLMTEALLVFSPESSLLHSLSRKGRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLVTRHGQAGLLAVLWAGLQCSGGVGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSASLLLGMCSLWFTASVTGAAWYLAVLCPVLTSLVIMNQVSNAYLYRKRIQP |
| Enzyme Length | 222 |
| Uniprot Accession Number | O14569 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-ascorbate(out) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; Evidence={ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525; Evidence={ECO:0000305|PubMed:23641721}; CATALYTIC ACTIVITY: Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3; Evidence={ECO:0000250|UniProtKB:Q9WUE3};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404; Evidence={ECO:0000250|UniProtKB:Q9WUE3}; |
| DNA Binding | |
| EC Number | 7.2.1.3 |
| Enzyme Function | FUNCTION: Transmembrane reductase that may use ascorbate as an electron donor in the cytoplasm and transfer electrons across endoplasmic reticulum membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in the lumen of that compartment. {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7 for the electron donation reaction to monodehydroascorbate reaction (PubMed:23641721). Optimum pH is around 6.5 for re-reduction reaction process of the oxidized heme with ascorbate (PubMed:23641721). {ECO:0000269|PubMed:23641721}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Topological domain (7); Transmembrane (6) |
| Keywords | Cytoplasmic vesicle;Direct protein sequencing;Electron transport;Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport |
| Interact With | Q3SXY8; P11912; O95471; Q86T13; O75208; Q96BA8; Q9Y282; Q5JX71; Q8TED1; P27815-4; O15173; P54829; Q96TC7; P54219-3; Q9BRI3; Q6P9G4; Q96B21 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16169070; 25814554; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,974 |
| Kinetics | |
| Metal Binding | METAL 48; /note=Iron 1 (heme b 1 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 86; /note=Iron 2 (heme b 2 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 120; /note=Iron 1 (heme b 1 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4; METAL 159; /note=Iron 2 (heme b 2 axial ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q53TN4 |
| Rhea ID | RHEA:66524; RHEA:66525; RHEA:30403; RHEA:30404 |
| Cross Reference Brenda |