Q8CI59 · STEA3_MOUSE

  • Protein
    Metalloreductase STEAP3
  • Gene
    Steap3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Integral membrane protein that functions as a NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe3+ chelate that is bound on the other side of the membrane (PubMed:16227996, PubMed:16609065, PubMed:18955558).
Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe3+ chelate (By similarity).
Can also reduce Cu2+ to Cu1+ (PubMed:16609065).
Mediates efficient transferrin-dependent iron uptake in erythroid cells (PubMed:16227996).
May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression (By similarity).
Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP (By similarity).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

heme b (UniProtKB | Rhea| CHEBI:60344 )

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site36-39NADP+ (UniProtKB | ChEBI)
Binding site58-59NADP+ (UniProtKB | ChEBI)
Binding site91-98NADP+ (UniProtKB | ChEBI)
Binding site116NADP+ (UniProtKB | ChEBI)
Binding site151NADP+ (UniProtKB | ChEBI)
Binding site152FAD (UniProtKB | ChEBI)
Binding site160FAD (UniProtKB | ChEBI)
Binding site229Fe3+ (UniProtKB | ChEBI)
Binding site281FAD (UniProtKB | ChEBI)
Binding site302FAD (UniProtKB | ChEBI)
Binding site303FAD (UniProtKB | ChEBI)
Binding site316Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site319Fe3+ (UniProtKB | ChEBI)
Site325-326Cleavage; by RHBDL4/RHBDD1
Binding site378FAD (UniProtKB | ChEBI)
Binding site395FAD (UniProtKB | ChEBI)
Binding site409Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentendosome
Cellular Componentendosome membrane
Cellular Componentmultivesicular body
Cellular Componentplasma membrane
Molecular Functioncupric reductase activity
Molecular FunctionFAD binding
Molecular Functionferric-chelate reductase (NADPH) activity
Molecular Functionferric-chelate reductase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processapoptotic process
Biological Processcopper ion import
Biological Processestablishment of localization in cell
Biological Processexosomal secretion
Biological Processiron import into cell
Biological Processiron ion import across cell outer membrane
Biological Processiron ion transport
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
Biological Processprotein secretion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Metalloreductase STEAP3
  • EC number
  • Alternative names
    • Dudulin-2
    • Protein nm1054
    • Six-transmembrane epithelial antigen of prostate 3
    • Tumor suppressor-activated pathway protein 6

Gene names

    • Name
      Steap3
    • Synonyms
      Tsap6

Organism names

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

Accessions

  • Primary accession
    Q8CI59
  • Secondary accessions
    • Q3TKE4
    • Q80ZF3
    • Q8C5F0
    • Q924Z1

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-207Cytoplasmic
Transmembrane208-228Helical
Topological domain229-258Vesicular
Transmembrane259-279Helical
Topological domain280-304Cytoplasmic
Transmembrane305-325Helical
Topological domain326-358Vesicular
Transmembrane359-379Helical
Topological domain380-390Cytoplasmic
Transmembrane391-411Helical
Topological domain412-433Vesicular
Transmembrane434-454Helical
Topological domain455-488Cytoplasmic

Keywords

Phenotypes & Variants

Involvement in disease

  • Defects in Steap3 are the cause of fragile-red phenotype characterized by hypochromic microcytic anemia

Disruption phenotype

Mice display iron deficiency anemia, due to a defect in iron release through the transferrin cycle.

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant288in fragile-red; loss of endosomal membrane localization; 2-fold decrease in ferric-chelate reductase activity
Mutagenesis316Loss of ferric-chelate reductase activity.
Mutagenesis409Loss of ferric-chelate reductase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00002851721-488Metalloreductase STEAP3
Modified residue11Phosphoserine
Modified residue17Phosphoserine
Modified residue20Phosphoserine
Glycosylation256N-linked (GlcNAc...) asparagine
Modified residue486Phosphoserine

Post-translational modification

Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner (By similarity).
Glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in fetal liver (the site of midgestational hematopoiesis).

Interaction

Subunit

Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain259-407Ferric oxidoreductase

Sequence similarities

Belongs to the STEAP family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8CI59-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    488
  • Mass (Da)
    54,749
  • Last updated
    2003-03-01 v1
  • Checksum
    9A08D99C90CF83F4
MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKEHLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICSDQPEAKRTISEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYTYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSLPSIANSLNWKEFSFVQSTLGFVALILSTMHTLTYGWTRAFEENHYKFYLPPTFTLTLLLPCVIILAKGLFLLPCLSRRLTKIRRGWEKDGAVKFMLPGDHTQGEKTSHV

Q8CI59-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0R4J1G9A0A0R4J1G9_MOUSESteap3488
D3YTP0D3YTP0_MOUSESteap3418
E9QN92E9QN92_MOUSESteap3526

Sequence caution

The sequence AAK50539.1 differs from that shown. Reason: Frameshift

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0248321in isoform 2
Sequence conflict81in Ref. 3; BAC37383
Sequence conflict157in Ref. 2; AAK50539
Sequence conflict169-172in Ref. 2; AAK50539
Sequence conflict176-179in Ref. 2; AAK50539
Sequence conflict212in Ref. 2; AAK50539
Sequence conflict350in Ref. 3; BAC37383/BAE39201
Sequence conflict455in Ref. 3; BAC37383/BAE39201

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY214462
EMBL· GenBank· DDBJ
AAO38239.1
EMBL· GenBank· DDBJ
mRNA
AY029586
EMBL· GenBank· DDBJ
AAK50539.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK078769
EMBL· GenBank· DDBJ
BAC37383.1
EMBL· GenBank· DDBJ
mRNA
AK167028
EMBL· GenBank· DDBJ
BAE39201.1
EMBL· GenBank· DDBJ
mRNA
AK171237
EMBL· GenBank· DDBJ
BAE42333.1
EMBL· GenBank· DDBJ
mRNA
BC037435
EMBL· GenBank· DDBJ
AAH37435.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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