Q8K385 · FRRS1_MOUSE

  • Protein
    Ferric-chelate reductase 1
  • Gene
    FRRS1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Ferric-chelate reductases reduce Fe3+ to Fe2+ before its transport from the endosome to the cytoplasm.

Cofactor

heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 2 heme b groups non-covalently.

Features

Showing features for binding site.

159250100150200250300350400450500550
TypeIDPosition(s)Description
Binding site373Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue
Binding site414Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue
Binding site446Fe (UniProtKB | ChEBI) of heme b 1 (UniProtKB | ChEBI); axial binding residue
Binding site482Fe (UniProtKB | ChEBI) of heme b 2 (UniProtKB | ChEBI); axial binding residue

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmembrane
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on metal ions
Biological Processintracellular iron ion homeostasis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ferric-chelate reductase 1
  • EC number
  • Alternative names
    • Stromal cell-derived receptor 2 (SDR-2)

Gene names

    • Name
      FRRS1
    • Synonyms
      Sdfr2, Sdr2

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8K385
  • Secondary accessions
    • P97301
    • Q3TJV0
    • Q3UMF5

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane2-22Helical; Name=1
Transmembrane372-392Helical; Name=2
Transmembrane415-435Helical; Name=3
Transmembrane446-466Helical; Name=4
Transmembrane477-499Helical; Name=5
Transmembrane515-535Helical; Name=6
Transmembrane569-589Helical; Name=7

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00003148441-592Ferric-chelate reductase 1
Glycosylation85N-linked (GlcNAc...) asparagine
Glycosylation308N-linked (GlcNAc...) asparagine
Glycosylation321N-linked (GlcNAc...) asparagine
Glycosylation353N-linked (GlcNAc...) asparagine

Keywords

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.

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-179Reelin
Domain216-331DOMON
Domain335-534Cytochrome b561

Sequence similarities

Belongs to the FRRS1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    592
  • Mass (Da)
    66,047
  • Last updated
    2002-10-01 v1
  • Checksum
    EAC9146163E85ED3
MAAPQITLSVLVIALLTCSVTAYPNGKVPMSCGGMIPQHNHSPQSEPIHQITVSQTTFKPGDQIEVTLSGPPFRGFLLEARDAENLSGPPIGSFTLIDSEESQLLTCTDVQGLAVSHTRSSKKTEIKVYWDAPSPAPDHIRFLATVVQKFKIYWVKIPSPVISQPNAPPFTTPKATTQPLTTPPSVSHLTKPFSAFECGNKKFCVRSPLNCDPEKEPACVFLSFTRDNQSVMVEMSGPSDGYVSFAFSHDQWMGDDDAYLCIREDQTVDIQPSYLTGRSYPVMDSRGTLEDMAWRLADGVIQCSFRRNITLPEAKNRFVLNESYYIFFAEGPSHDGRIFRHSQQPLITYEKYNVTDTPKSVGGSRSSPLLKAHGALMFVAWMTTVSIGVLVARFFRSVWSKAFFLREAAWFQVHRMLMVATSLLTCVAFVLPFVYRGGWSWRAGYHPYLGCTVMTLAVLQPLLATFRPPLHDPRRQVFNWTHWSVGTAARIIAVAAMFLGMDLPGLNLPSPQKTYAMMGFVVWHIGTEVILEIHAYRLSRKVEILDNDRIQILQSLTVAEAEGHVFKKVVLAVYICGNVIFLSIFLSAINHI

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JGF6A0A0G2JGF6_MOUSEFrrs184
A0A0G2JFP4A0A0G2JFP4_MOUSEFrrs1592
A0A0G2JEJ3A0A0G2JEJ3_MOUSEFrrs1123

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict9in Ref. 1; BAA09055
Sequence conflict61in Ref. 1; BAA09055
Sequence conflict65in Ref. 2; BAE26143/BAE39395/BAE37025
Sequence conflict272in Ref. 2; BAE39395/BAE37025
Sequence conflict299in Ref. 2; BAE39395/BAE37025
Sequence conflict419in Ref. 1; BAA09055
Sequence conflict428in Ref. 1; BAA09055

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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