P53746 · FRE4_YEAST
- ProteinFerric reductase transmembrane component 4
- GeneFRE4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids719 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe3+ bound to dihydroxamate rhodotorulic acid. Fe3+ is reduced to Fe2+, which then dissociates from the siderophore and can be imported by the high-affinity Fe2+ transport complex in the plasma membrane.
Catalytic activity
- 2 a Fe(II)-siderophore + H+ + NADP+ = 2 a Fe(III)-siderophore + NADPH
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 309 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 323 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 379 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 393 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 472-478 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HPFTVMD | ||||||
Binding site | 519-522 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GPYG | ||||||
Binding site | 685-686 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: CG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ferric-chelate reductase (NADPH) activity | |
Molecular Function | ferric-chelate reductase activity | |
Molecular Function | metal ion binding | |
Biological Process | copper ion import | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | iron ion transport | |
Biological Process | siderophore transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerric reductase transmembrane component 4
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP53746
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-156 | Extracellular | ||||
Sequence: KAPPSKTSLINTHERRSIYSCYVGLRKETWGFNGSAICRYEPAIQSMLYCLYEDTHEKGYSNKTLEKGFEEMRQFCYTPKFLNMTDAEFYTSLDNGTYYIQDQPKAGINITYPIRLNTTLRKAYYDAYYGYYYNHDIP | ||||||
Transmembrane | 157-177 | Helical; Name=1 | ||||
Sequence: YYFGGIICAYFVGVMLLAGLI | ||||||
Topological domain | 178-228 | Cytoplasmic | ||||
Sequence: RFLNYTPIKKIMFQQKLVNYVRGYTTLPTLYEKHAEPFSYLKVITGYLPTR | ||||||
Transmembrane | 229-249 | Helical; Name=2 | ||||
Sequence: FETLVILGYLILHTIFMAYKY | ||||||
Topological domain | 250-267 | Extracellular | ||||
Sequence: QYDPYHIIFAAHRAEVAH | ||||||
Transmembrane | 268-288 | Helical; Name=3 | ||||
Sequence: FVAYRSGILSFAHLPLIVLFA | ||||||
Topological domain | 289-304 | Cytoplasmic | ||||
Sequence: GRNNFLQLISGLKHTS | ||||||
Transmembrane | 305-325 | Helical; Name=4 | ||||
Sequence: FIVFHKWLGRMMFLDAIIHAA | ||||||
Topological domain | 326-346 | Extracellular | ||||
Sequence: GFTNYYLYYKKWNTVRLRVYW | ||||||
Transmembrane | 347-367 | Helical; Name=5 | ||||
Sequence: KFGIATTCLAGMLIFFSIAAF | ||||||
Topological domain | 368-373 | Cytoplasmic | ||||
Sequence: RRHYYE | ||||||
Transmembrane | 374-394 | Helical; Name=6 | ||||
Sequence: TFMALHIVFAALFLYTCWEHV | ||||||
Topological domain | 395 | Extracellular | ||||
Sequence: T | ||||||
Transmembrane | 396-416 | Helical; Name=7 | ||||
Sequence: NFSGIEWIYAAIAIWGVDRIV | ||||||
Topological domain | 417-719 | Cytoplasmic | ||||
Sequence: RITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTAHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKKELMALKGLNVQVHIYNSKQELASAEKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELPLSLNDTSISDLEFATFHVGRPNVEEILNESVNHSGSLAVVCCGPPIFVDTARNQTAKAVIRNPSRMIEYLEEYQAW |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLLVHIISFLLFFQLSAA | ||||||
Chain | PRO_0000010140 | 19-719 | Ferric reductase transmembrane component 4 | |||
Sequence: KAPPSKTSLINTHERRSIYSCYVGLRKETWGFNGSAICRYEPAIQSMLYCLYEDTHEKGYSNKTLEKGFEEMRQFCYTPKFLNMTDAEFYTSLDNGTYYIQDQPKAGINITYPIRLNTTLRKAYYDAYYGYYYNHDIPYYFGGIICAYFVGVMLLAGLIRFLNYTPIKKIMFQQKLVNYVRGYTTLPTLYEKHAEPFSYLKVITGYLPTRFETLVILGYLILHTIFMAYKYQYDPYHIIFAAHRAEVAHFVAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYYKKWNTVRLRVYWKFGIATTCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTCWEHVTNFSGIEWIYAAIAIWGVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTAHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKKELMALKGLNVQVHIYNSKQELASAEKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELPLSLNDTSISDLEFATFHVGRPNVEEILNESVNHSGSLAVVCCGPPIFVDTARNQTAKAVIRNPSRMIEYLEEYQAW | ||||||
Glycosylation | 51 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 80 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 101 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 127 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 135 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By iron deprivation.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 273-407 | Ferric oxidoreductase | ||||
Sequence: SGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYYKKWNTVRLRVYWKFGIATTCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTCWEHVTNFSGIEWIYAAI | ||||||
Domain | 408-527 | FAD-binding FR-type | ||||
Sequence: AIWGVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTA | ||||||
Region | 606-643 | Disordered | ||||
Sequence: EKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELP |
Sequence similarities
Belongs to the ferric reductase (FRE) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length719
- Mass (Da)82,015
- Last updated1996-10-01 v1
- Checksum9CA91F1F890AF1F9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z71675 EMBL· GenBank· DDBJ | CAA96342.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10601.1 EMBL· GenBank· DDBJ | Genomic DNA |