P78588 (FREL_CANAX) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable ferric reductase transmembrane component EC=1.16.1.7 Alternative name(s): Ferric-chelate reductase | ||
| Gene names |
| ||
| Organism | Candida albicans (Yeast) | ||
| Taxonomic identifier | 5476 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 669 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2 Fe2+ + NAD+ + H+ = 2 Fe3+ + NADH. |
| Cofactor | FAD Probable. |
| Subcellular location | Membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the ferric reductase (FRE) family. Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Ion transport Iron transport Transport |
| Cellular component | Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | FAD Iron NAD |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW ion transportInferred from electronic annotation. Source: UniProtKB-KW iron ion homeostasisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro ferric-chelate reductase activityInferred from electronic annotation. Source: EC flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 669 | 669 | Probable ferric reductase transmembrane component | PRO_0000210151 | |||||
Regions | |||||||||
| Transmembrane | 122 – 142 | 21 | Helical; Potential | ||||||
| Transmembrane | 198 – 218 | 21 | Helical; Potential | ||||||
| Transmembrane | 234 – 254 | 21 | Helical; Potential | ||||||
| Transmembrane | 281 – 301 | 21 | Helical; Potential | ||||||
| Transmembrane | 313 – 333 | 21 | Helical; Potential | ||||||
| Transmembrane | 340 – 360 | 21 | Helical; Potential | ||||||
| Transmembrane | 499 – 519 | 21 | Helical; Potential | ||||||
| Domain | 239 – 373 | 135 | Ferric oxidoreductase | ||||||
| Domain | 374 – 492 | 119 | FAD-binding FR-type | ||||||
| Nucleotide binding | 437 – 442 | 6 | FAD Potential | ||||||
| Compositional bias | 65 – 77 | 13 | Poly-Ser | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 20 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 52 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 64 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 116 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 152 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 524 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 653 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans." Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M., Yamada-Okabe H. Microbiology 142:2515-2523(1996) [PubMed: 8828219] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D83181 Genomic DNA. Translation: BAA11834.1. |
3D structure databases | |
| ProteinModelPortal | P78588. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR013112. FAD-bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013121. Fe_red_NAD-bd_6. IPR013130. Flavoprotein_TM. [Graphical view] |
| Pfam | PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view] |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FREL_CANAX | ||||||||
| Accession | Primary (citable) accession number: P78588 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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