STEAP3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2VNS, 2VQ3

Identifiers

Aliases

STEAP3, AHMIO2, STMP3, TSAP6, dudlin-2, dudulin-2, pHyde, STEAP3 metalloreductase

External IDs

MGI: 1915678 HomoloGene: 10084 GeneCards: STEAP3

Gene ontology
Molecular function	• oxidoreductase activity • protein binding • ferric-chelate reductase (NADPH) activity • metal ion binding • cupric reductase activity • oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor
Cellular component	• integral component of membrane • multivesicular body • endosome • endosome membrane • membrane • integral component of plasma membrane • cytoplasm
Biological process	• apoptotic process • protein secretion • cell cycle • iron ion homeostasis • copper ion import • ion transport • oxidation-reduction process • transferrin transport • transport • ferric iron import into cell • regulation of apoptotic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


55240


68428

Ensembl


ENSG00000115107


ENSMUSG00000026389

UniProt


Q658P3


Q8CI59

RefSeq (mRNA)


NM_001008410 NM_018234 NM_138637 NM_182915


NM_001085409 NM_133186

RefSeq (protein)


NP_001008410.1 NP_060704.2 NP_619543.2 NP_878919.2


NP_001078878.1 NP_573449.2

Location (UCSC)

Chr 2: 119.22 – 119.27 Mb

Chr 1: 120.19 – 120.27 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Metalloreductase STEAP3 is an enzyme that in humans is encoded by the STEAP3 gene.^[3]^[4]

STEAP3 is a metalloreductase, capable of coverting iron from an insoluble ferric (Fe³⁺) to a soluble ferrous (Fe²⁺) form.^[5]

Interactions

STEAP3 has been shown to interact with BNIP3L^[3] and PKMYT1.^[3]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 3 Passer BJ, Nancy-Portebois V, Amzallag N, Prieur S, Cans C, Roborel de Climens A, Fiucci G, Bouvard V, Tuynder M, Susini L, Morchoisne S, Crible V, Lespagnol A, Dausset J, Oren M, Amson R, Telerman A (Mar 2003). "The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase". Proc Natl Acad Sci U S A. 100 (5): 2284–9. doi:10.1073/pnas.0530298100. PMC 151332. PMID 12606722.
↑ "Entrez Gene: STEAP3 STEAP family member 3".
↑ Ohgami RS, Campagna DR, McDonald A, Fleming MD (August 2006). "The Steap proteins are metalloreductases". Blood. 108 (4): 1388–94. doi:10.1182/blood-2006-02-003681. PMC 1785011. PMID 16609065.

Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Korkmaz KS, Elbi C, Korkmaz CG, Loda M, Hager GL, Saatcioglu F (2002). "Molecular cloning and characterization of STAMP1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer.". J. Biol. Chem. 277 (39): 36689–96. doi:10.1074/jbc.M202414200. PMID 12095985.
Amzallag N, Passer BJ, Allanic D, Segura E, Théry C, Goud B, Amson R, Telerman A (2004). "TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway.". J. Biol. Chem. 279 (44): 46104–12. doi:10.1074/jbc.M404850200. PMID 15319436.
Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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STEAP3

Interactions

References

Further reading