Protein detail
STEA4
Metalloreductase STEAP4 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 4) (SixTransMembrane protein of prostate 2) (Tumor necrosis factor, alpha-induced protein 9)
Entry name STEA4 | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 1 | Transmembrane count 6 | Protein classification |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information8
Protein Names
Metalloreductase STEAP4 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 4) (SixTransMembrane protein of prostate 2) (Tumor necrosis factor, alpha-induced protein 9)
Protein Function (3)
- Transporters:Transport Electron Carriers
- Enzymes
- ENZYME proteins:Oxidoreductases
Transmembrane
202..224; Helical; 236..256; Helical; 293..313; Helical; 342..362; Helical; 381..401; Helical; 419..439; Helical
Transmembrane Count
6
Ensembl
Entrez Gene Symbol
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization1
Cell SpecificChoroid plexus epithelial cells
Function & Pathway6
Protein Function (3)
- Transporters:Transport Electron Carriers
- Enzymes
- ENZYME proteins:Oxidoreductases
Cellular Component (8)
Molecular Function (6)
Biological Process (3)
Reactome (3)
Mediation Categories
Fusion and delivery mediation
Relations & Evidence22
Ligand-Receptor Signaling (20)
20 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| extracellular | extracellular | OmniPath | No | No | No | Yes | No |
| intracellular | intracellular | GO_Intercell | No | No | No | Yes | No |
| intracellular | intracellular | UniProt_location | No | No | No | Yes | No |
| intracellular | intracellular | OmniPath | No | No | No | Yes | No |
| transporter | transporter | Surfaceome | No | Yes | No | Yes | No |
| steap | transporter | Surfaceome | No | Yes | No | Yes | No |
| transporter | transporter | OmniPath | No | Yes | No | Yes | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | Yes | No |
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Protein Complex Composition (1)
Sequence, Structure & Domains12
Sequences
Length
459
Mass
51,981
Sequence
MEKTCIDALPLTMNSSEKQETVCIFGTGDFGRSLGLKMLQCGYSVVFGSRNPQKTTLLPSGAEVLSYSEAAKKSGIIIIAIHREHYDFLTELTEVLNGKILVDISNNLKINQYPESNAEYLAHLVPGAHVVKAFNTISAWALQSGALDASRQVFVCGNDSKAKQRVMDIVRNLGLTPMDQGSLMAAKEIEKYPLQLFPMWRFPFYLSAVLCVFLFFYCVIRDVIYPYVYEKKDNTFRMAISIPNRIFPITALTLLALVYLPGVIAAILQLYRGTKYRRFPDWLDHWMLCRKQLGLVALGFAFLHVLYTLVIPIRYYVRWRLGNLTVTQAILKKENPFSTSSAWLSDSYVALGILGFFLFVLLGITSLPSVSNAVNWREFRFVQSKLGYLTLILCTAHTLVYGGKRFLSPSNLRWYLPAAYVLGLIIPCTVLVIKFVLIMPCVDNTLTRIRQGWERNSKH
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q687X5-1; Sequence=Displayed; Name=2; IsoId=Q687X5-2; Sequence=VSP_024833
Alternative Sequence
153..328; Missing (in isoform 2)
3D Structural Models
Turn
40..42; 71..73; 93..95; 239..242; 368..370; 404..407
Helix
29..39; 67..70; 87..92; 117..124; 139..144; 160..172; 183..185; 186..191; 192..194; 201..222; 225..228; 236..238; 243..256; 261..272; 283..287; 290..308; 311..313; 315..330; 339..365; 376..383; 385..403; 425..438; 440..449
Beta Strand
21..25; 44..48; 75..79; 100..103; 112..115; 128..132; 134..137; 148..150; 152..158; 176..179; 196..198; 275..277; 371..374; 413..415; 419..422
3D Structure
Electron microscopy (2)
Domain & Motif Annotations
Domain (FT)
247..395; Ferric oxidoreductase
Protein Families
STEAP family
Sequence Similarities
Belongs to the STEAP family.
Supporting Publications1
| PMID | Title | Abstract |
|---|---|---|
| 26739763 | Triple SILAC quantitative proteomic analysis reveals differential abundance of cell signaling proteins between normal and lung cancer-derived exosomes. | Proteins associated with signal transduction, including EGFR, GRB2 and SRC, were enriched in NSCLC exosomes, and could actively regulate cell proliferation in recipient cells. To better understand the role of these microvesicles in lung carcinogenesis, we employed a Triple SILAC quantitative proteomic strategy to examine the differential protein abundance between exosomes derived from an immortalized normal bronchial epithelial cell line and two non-small cell lung cancer (NSCLC) cell lines harboring distinct activating mutations in the cell signaling molecules: Kirsten rat sarcoma viral oncogene homolog (KRAS) or epidermal growth factor receptor (EGFR). |