Q8CI59 · STEA3_MOUSE
- ProteinMetalloreductase STEAP3
- GeneSteap3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids488 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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
- 2 Fe2+ + H+ + NADP+ = 2 Fe3+ + NADPHThis reaction proceeds in the backward direction.
- 2 Cu+ + H+ + NADP+ = 2 Cu2+ + NADPHThis reaction proceeds in the backward direction.
Cofactor
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36-39 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SGDF | ||||||
Binding site | 58-59 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 91-98 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VFREHYSS | ||||||
Binding site | 116 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 151 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 152 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 160 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 229 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 281 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 302 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 303 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 316 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 319 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 325-326 | Cleavage; by RHBDL4/RHBDD1 | ||||
Sequence: LR | ||||||
Binding site | 378 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 395 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 409 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome | |
Cellular Component | endosome membrane | |
Cellular Component | multivesicular body | |
Cellular Component | plasma membrane | |
Molecular Function | cupric reductase activity | |
Molecular Function | FAD binding | |
Molecular Function | ferric-chelate reductase (NADPH) activity | |
Molecular Function | ferric-chelate reductase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | apoptotic process | |
Biological Process | copper ion import | |
Biological Process | establishment of localization in cell | |
Biological Process | exosomal secretion | |
Biological Process | iron import into cell | |
Biological Process | iron ion import across cell outer membrane | |
Biological Process | iron ion transport | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator | |
Biological Process | protein secretion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetalloreductase STEAP3
- 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 accessionQ8CI59
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-207 | Cytoplasmic | ||||
Sequence: MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKEHLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICSDQPEAKRTISEMARAMGFTPLDMGSLASAREVEAIPLR | ||||||
Transmembrane | 208-228 | Helical | ||||
Sequence: LLPSWKVPTLLALGLFVCFYT | ||||||
Topological domain | 229-258 | Vesicular | ||||
Sequence: YNFIRDVLQPYIRKDENKFYKMPLSVVNTT | ||||||
Transmembrane | 259-279 | Helical | ||||
Sequence: LPCVAYVLLSLVYLPGVLAAA | ||||||
Topological domain | 280-304 | Cytoplasmic | ||||
Sequence: LQLRRGTKYQRFPDWLDHWLQHRKQ | ||||||
Transmembrane | 305-325 | Helical | ||||
Sequence: IGLLSFFFAMLHALYSFCLPL | ||||||
Topological domain | 326-358 | Vesicular | ||||
Sequence: RRSHRYDLVNLAVKQVLANKSRLWVEEEVWRME | ||||||
Transmembrane | 359-379 | Helical | ||||
Sequence: IYLSLGVLALGMLSLLAVTSL | ||||||
Topological domain | 380-390 | Cytoplasmic | ||||
Sequence: PSIANSLNWKE | ||||||
Transmembrane | 391-411 | Helical | ||||
Sequence: FSFVQSTLGFVALILSTMHTL | ||||||
Topological domain | 412-433 | Vesicular | ||||
Sequence: TYGWTRAFEENHYKFYLPPTFT | ||||||
Transmembrane | 434-454 | Helical | ||||
Sequence: LTLLLPCVIILAKGLFLLPCL | ||||||
Topological domain | 455-488 | Cytoplasmic | ||||
Sequence: SRRLTKIRRGWEKDGAVKFMLPGDHTQGEKTSHV |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Disruption phenotype
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 288 | in fragile-red; loss of endosomal membrane localization; 2-fold decrease in ferric-chelate reductase activity | ||||
Sequence: Y → H | ||||||
Mutagenesis | 316 | Loss of ferric-chelate reductase activity. | ||||
Sequence: H → L | ||||||
Mutagenesis | 409 | Loss of ferric-chelate reductase activity. | ||||
Sequence: H → L |
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.
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000285172 | 1-488 | Metalloreductase STEAP3 | |||
Sequence: MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKEHLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICSDQPEAKRTISEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYTYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSLPSIANSLNWKEFSFVQSTLGFVALILSTMHTLTYGWTRAFEENHYKFYLPPTFTLTLLLPCVIILAKGLFLLPCLSRRLTKIRRGWEKDGAVKFMLPGDHTQGEKTSHV | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 17 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 486 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 259-407 | Ferric oxidoreductase | ||||
Sequence: LPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSLPSIANSLNWKEFSFVQSTLGFVALILST |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length488
- Mass (Da)54,749
- Last updated2003-03-01 v1
- Checksum9A08D99C90CF83F4
Q8CI59-2
- Name2
- Differences from canonical
- 1-1: M → MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1G9 | A0A0R4J1G9_MOUSE | Steap3 | 488 | ||
D3YTP0 | D3YTP0_MOUSE | Steap3 | 418 | ||
E9QN92 | E9QN92_MOUSE | Steap3 | 526 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_024832 | 1 | in isoform 2 | |||
Sequence: M → MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM | ||||||
Sequence conflict | 81 | in Ref. 3; BAC37383 | ||||
Sequence: V → M | ||||||
Sequence conflict | 157 | in Ref. 2; AAK50539 | ||||
Sequence: G → V | ||||||
Sequence conflict | 169-172 | in Ref. 2; AAK50539 | ||||
Sequence: SDQP → GNQQ | ||||||
Sequence conflict | 176-179 | in Ref. 2; AAK50539 | ||||
Sequence: RTIS → QRVM | ||||||
Sequence conflict | 212 | in Ref. 2; AAK50539 | ||||
Sequence: W → G | ||||||
Sequence conflict | 350 | in Ref. 3; BAC37383/BAE39201 | ||||
Sequence: V → A | ||||||
Sequence conflict | 455 | in Ref. 3; BAC37383/BAE39201 | ||||
Sequence: S → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |