Q8K385 · FRRS1_MOUSE
- ProteinFerric-chelate reductase 1
- GeneFRRS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids592 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Ferric-chelate reductases reduce Fe3+ to Fe2+ before its transport from the endosome to the cytoplasm.
Cofactor
Note: Binds 2 heme b groups non-covalently.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 373 | Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 414 | Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 446 | Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 482 | Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on metal ions | |
Biological Process | intracellular iron ion homeostasis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerric-chelate reductase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8K385
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 2-22 | Helical; Name=1 | ||||
Sequence: AAPQITLSVLVIALLTCSVTA | ||||||
Transmembrane | 372-392 | Helical; Name=2 | ||||
Sequence: AHGALMFVAWMTTVSIGVLVA | ||||||
Transmembrane | 415-435 | Helical; Name=3 | ||||
Sequence: RMLMVATSLLTCVAFVLPFVY | ||||||
Transmembrane | 446-466 | Helical; Name=4 | ||||
Sequence: HPYLGCTVMTLAVLQPLLATF | ||||||
Transmembrane | 477-499 | Helical; Name=5 | ||||
Sequence: VFNWTHWSVGTAARIIAVAAMFL | ||||||
Transmembrane | 515-535 | Helical; Name=6 | ||||
Sequence: YAMMGFVVWHIGTEVILEIHA | ||||||
Transmembrane | 569-589 | Helical; Name=7 | ||||
Sequence: VVLAVYICGNVIFLSIFLSAI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000314844 | 1-592 | Ferric-chelate reductase 1 | |||
Sequence: MAAPQITLSVLVIALLTCSVTAYPNGKVPMSCGGMIPQHNHSPQSEPIHQITVSQTTFKPGDQIEVTLSGPPFRGFLLEARDAENLSGPPIGSFTLIDSEESQLLTCTDVQGLAVSHTRSSKKTEIKVYWDAPSPAPDHIRFLATVVQKFKIYWVKIPSPVISQPNAPPFTTPKATTQPLTTPPSVSHLTKPFSAFECGNKKFCVRSPLNCDPEKEPACVFLSFTRDNQSVMVEMSGPSDGYVSFAFSHDQWMGDDDAYLCIREDQTVDIQPSYLTGRSYPVMDSRGTLEDMAWRLADGVIQCSFRRNITLPEAKNRFVLNESYYIFFAEGPSHDGRIFRHSQQPLITYEKYNVTDTPKSVGGSRSSPLLKAHGALMFVAWMTTVSIGVLVARFFRSVWSKAFFLREAAWFQVHRMLMVATSLLTCVAFVLPFVYRGGWSWRAGYHPYLGCTVMTLAVLQPLLATFRPPLHDPRRQVFNWTHWSVGTAARIIAVAAMFLGMDLPGLNLPSPQKTYAMMGFVVWHIGTEVILEIHAYRLSRKVEILDNDRIQILQSLTVAEAEGHVFKKVVLAVYICGNVIFLSIFLSAINHI | ||||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 308 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 321 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in spleen, liver and kidney with low expression in brain. Localizes in adult brain to the choroid plexus of the fourth, third, and lateral ventricles and to ependymal cells that line the ventricles.
Induction
Down-regulated in kidney and liver of mice lacking hypotransferrinemic (hpx), which have iron overload of the liver and pancreas.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-179 | Reelin | ||||
Sequence: IALLTCSVTAYPNGKVPMSCGGMIPQHNHSPQSEPIHQITVSQTTFKPGDQIEVTLSGPPFRGFLLEARDAENLSGPPIGSFTLIDSEESQLLTCTDVQGLAVSHTRSSKKTEIKVYWDAPSPAPDHIRFLATVVQKFKIYWVKIPSPVISQPNAPPFTTPKATTQP | ||||||
Domain | 216-331 | DOMON | ||||
Sequence: EPACVFLSFTRDNQSVMVEMSGPSDGYVSFAFSHDQWMGDDDAYLCIREDQTVDIQPSYLTGRSYPVMDSRGTLEDMAWRLADGVIQCSFRRNITLPEAKNRFVLNESYYIFFAEG | ||||||
Domain | 335-534 | Cytochrome b561 | ||||
Sequence: DGRIFRHSQQPLITYEKYNVTDTPKSVGGSRSSPLLKAHGALMFVAWMTTVSIGVLVARFFRSVWSKAFFLREAAWFQVHRMLMVATSLLTCVAFVLPFVYRGGWSWRAGYHPYLGCTVMTLAVLQPLLATFRPPLHDPRRQVFNWTHWSVGTAARIIAVAAMFLGMDLPGLNLPSPQKTYAMMGFVVWHIGTEVILEIH |
Sequence similarities
Belongs to the FRRS1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length592
- Mass (Da)66,047
- Last updated2002-10-01 v1
- ChecksumEAC9146163E85ED3
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JGF6 | A0A0G2JGF6_MOUSE | Frrs1 | 84 | ||
A0A0G2JFP4 | A0A0G2JFP4_MOUSE | Frrs1 | 592 | ||
A0A0G2JEJ3 | A0A0G2JEJ3_MOUSE | Frrs1 | 123 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 1; BAA09055 | ||||
Sequence: S → R | ||||||
Sequence conflict | 61 | in Ref. 1; BAA09055 | ||||
Sequence: G → E | ||||||
Sequence conflict | 65 | in Ref. 2; BAE26143/BAE39395/BAE37025 | ||||
Sequence: E → K | ||||||
Sequence conflict | 272 | in Ref. 2; BAE39395/BAE37025 | ||||
Sequence: P → S | ||||||
Sequence conflict | 299 | in Ref. 2; BAE39395/BAE37025 | ||||
Sequence: G → S | ||||||
Sequence conflict | 419 | in Ref. 1; BAA09055 | ||||
Sequence: V → I | ||||||
Sequence conflict | 428 | in Ref. 1; BAA09055 | ||||
Sequence: A → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D50464 EMBL· GenBank· DDBJ | BAA09055.1 EMBL· GenBank· DDBJ | mRNA | ||
AK144933 EMBL· GenBank· DDBJ | BAE26143.1 EMBL· GenBank· DDBJ | mRNA | ||
AK162693 EMBL· GenBank· DDBJ | BAE37025.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167289 EMBL· GenBank· DDBJ | BAE39395.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027770 EMBL· GenBank· DDBJ | AAH27770.1 EMBL· GenBank· DDBJ | mRNA |