| IED ID | IndEnz0002001052 |
| Enzyme Type ID | protease001052 |
| Protein Name |
Metalloreductase STEAP3 EC 1.16.1.- Dudulin-2 Six-transmembrane epithelial antigen of prostate 3 Tumor suppressor-activated pathway protein 6 hTSAP6 pHyde hpHyde |
| Gene Name | STEAP3 TSAP6 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIYLSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHALAEKTSHV |
| Enzyme Length | 488 |
| Uniprot Accession Number | Q658P3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 116; /note=NADP; via amide nitrogen; /evidence=ECO:0000269|PubMed:18495927; BINDING 151; /note=NADP; via amide nitrogen; /evidence=ECO:0000269|PubMed:18495927; BINDING 152; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5; BINDING 160; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5; BINDING 281; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5; BINDING 302; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5; BINDING 378; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5; BINDING 395; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q687X5 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.16.1.- |
| Enzyme Function | FUNCTION: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP. {ECO:0000269|PubMed:15319436, ECO:0000269|PubMed:16651434}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 36..39; /note="NADP"; /evidence="ECO:0000269|PubMed:18495927, ECO:0007744|PDB:2VQ3"; NP_BIND 58..59; /note="NADP"; /evidence="ECO:0000269|PubMed:18495927, ECO:0007744|PDB:2VQ3"; NP_BIND 91..98; /note="NADP"; /evidence="ECO:0000269|PubMed:18495927, ECO:0007744|PDB:2VQ3" |
| Features | Alternative sequence (3); Beta strand (8); Binding site (8); Chain (1); Domain (1); Glycosylation (2); Helix (12); Metal binding (2); Modified residue (5); Mutagenesis (3); Natural variant (1); Nucleotide binding (3); Sequence conflict (8); Site (1); Topological domain (7); Transmembrane (6) |
| Keywords | 3D-structure;Alternative splicing;Apoptosis;Cell cycle;Copper;Endosome;FAD;Flavoprotein;Glycoprotein;Heme;Ion transport;Iron;Iron transport;Membrane;Metal-binding;NADP;Oxidoreductase;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With | Itself |
| Induction | INDUCTION: By p53/TP53. {ECO:0000269|PubMed:12606722}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to vesicular-like structures at the plasma membrane and around the nucleus. |
| Modified Residue | MOD_RES 11; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 17; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 20; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 474; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 486; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
| Post Translational Modification | PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner. {ECO:0000269|PubMed:22624035}.; PTM: Glycosylated. {ECO:0000269|PubMed:22624035}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2VNS; 2VQ3; |
| Mapped Pubmed ID | 10490598; 10699464; 10724160; 10873802; 10967094; 11185749; 11696321; 11756552; 11773441; 11784792; 11804587; 11948177; 12242347; 12456725; 12464619; 12773384; 12860998; 12907671; 15260990; 15994289; 16609065; 16630611; 17064668; 17244649; 17916560; 18218625; 18617898; 19236508; 20233848; 20379614; 20587610; 21119010; 21871451; 21988832; 22608513; 22665057; 22970203; 22971344; 23416715; 24355937; 24584464; 25080938; 25668492; 25963737; 26299518; 26598554; 26638075; 26675350; 27278019; 27825812; 28303916; 28486133; 28825699; 28860633; 30061681; 31176711; 31350307; 31871319; 32302585; 8662891; 8670801; 8756646; 8798539; 8805223; 8816443; 9013646; 9405671; 9829970; 9843499; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,601 |
| Kinetics | |
| Metal Binding | METAL 316; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:Q687X5; METAL 409; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:Q687X5 |
| Rhea ID | |
| Cross Reference Brenda |