STEAP3

STEAP3
Available structures
PDB	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	OMIM: 609671 MGI: 1915678 HomoloGene: 10084 GeneCards: STEAP3
Gene location (Human)
Chr.	Chromosome 2 (human)
End	119,265,652 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	120,200,435 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; spinal ganglia; ; bronchial epithelial cell; ; lactiferous duct; ; trigeminal ganglion; ; triceps brachii muscle; ; biceps brachii; ; thoracic diaphragm; ; vastus lateralis muscle; ; parotid gland;
	Top expressed in
	lip; ; aortic valve; ; membranous bone; ; ascending aorta; ; morula; ; human mandible; ; esophagus; ; maxilla; ; skeletal muscle tissue; ; yolk sac;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; protein binding; ferric-chelate reductase (NADPH) activity; metal ion binding; cupric reductase activity; oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor; identical protein binding;
Cellular component	integral component of membrane; multivesicular body; endosome; endosome membrane; membrane; integral component of plasma membrane; cytoplasm; plasma membrane;
Biological process	apoptotic process; protein secretion; cell cycle; iron ion homeostasis; copper ion import; ion transport; transferrin transport; regulation of apoptotic process; iron ion import across cell outer membrane;
	Sources:Amigo / QuickGO
Orthologs
	55240
	68428
	ENSG00000115107
	ENSMUSG00000026389
	Q658P3
	Q8CI59
	NM_001008410; NM_018234; NM_138637; NM_182915
	NM_001085409; NM_133186; NM_001379354; NM_001379355
	NP_001008410; NP_060704; NP_619543; NP_878919
	NP_001078878; NP_573449; NP_001366283; NP_001366284
	Wikidata
View/Edit Human	View/Edit Mouse

Metalloreductase STEAP3 is an enzyme that in humans is encoded by the STEAP3 gene.^[5]^[6]

STEAP3 is a metalloreductase, capable of converting iron from an insoluble ferric (Fe³⁺) to a soluble ferrous (Fe²⁺) form.^[7]

STEAP3 and other STEAP protein, with the exception of STEAP1, are predicted to contain a Di-nucleotide binding domain (Rossmann Fold). This has been shown using X-ray crystallography in the cases of STEAP3 and STEAP4 (PDB: 2VNS, 2VQ3 and 2YJZ).^[8]^[9]

Interactions

STEAP3 has been shown to interact with BNIP3L^[5] and PKMYT1.^[5]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000115107 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026389 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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 (March 2003). "The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase". Proceedings of the National Academy of Sciences of the United States of America. 100 (5): 2284–9. Bibcode:2003PNAS..100.2284P. 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.
↑ Sendamarai AK, Ohgami RS, Fleming MD, Lawrence CM (May 2008). "Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle" (PDF). Proceedings of the National Academy of Sciences of the United States of America. 105 (21): 7410–5. Bibcode:2008PNAS..105.7410S. doi:10.1073/pnas.0801318105. PMC 2396704. PMID 18495927.
↑ Gauss GH, Kleven MD, Sendamarai AK, Fleming MD, Lawrence CM (July 2013). "The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site". The Journal of Biological Chemistry. 288 (28): 20668–82. doi:10.1074/jbc.M113.479154. PMC 3711330. PMID 23733181.

Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 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 (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 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 (September 2002). "Molecular cloning and characterization of STAMP1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer". The Journal of Biological Chemistry. 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 (October 2004). "TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway". The Journal of Biological Chemistry. 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 (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 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 (January 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000115107 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026389 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12606722-5] 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 (March 2003). "The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase". Proceedings of the National Academy of Sciences of the United States of America. 100 (5): 2284–9. Bibcode:2003PNAS..100.2284P. doi:10.1073/pnas.0530298100. PMC 151332. PMID 12606722.

[entrez-6] "Entrez Gene: STEAP3 STEAP family member 3".

[pmid16609065-7] 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.

[8] Sendamarai AK, Ohgami RS, Fleming MD, Lawrence CM (May 2008). "Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle" (PDF). Proceedings of the National Academy of Sciences of the United States of America. 105 (21): 7410–5. Bibcode:2008PNAS..105.7410S. doi:10.1073/pnas.0801318105. PMC 2396704. PMID 18495927.

[9] Gauss GH, Kleven MD, Sendamarai AK, Fleming MD, Lawrence CM (July 2013). "The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site". The Journal of Biological Chemistry. 288 (28): 20668–82. doi:10.1074/jbc.M113.479154. PMC 3711330. PMID 23733181.

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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 (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a 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 Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Interactions

References

Further reading