Q8CIZ9 · NOX1_MOUSE
- ProteinNADPH oxidase 1
- GeneNox1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids591 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform 1
NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor.
Isoform 2
NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor.
Catalytic activity
Cofactor
Activity regulation
Isoform 2
The oxidase activity is potentiated by NOXA1 and NOXO1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 129 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 143 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 236 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 248 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 365-371 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HPFTLTS |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNADPH oxidase 1
- EC number
- Short namesNOX-1
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 accessionQ8CIZ9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell projection, invadopodium membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-36 | Cytoplasmic | ||||
Sequence: MAGELRGSRGPLQRIQIAPREAPNLHLTMGNWLVNH | ||||||
Transmembrane | 37-59 | Helical; Name=1 | ||||
Sequence: WLSVLFLVSWLGLNIFLFVYAFL | ||||||
Topological domain | 60-72 | Extracellular | ||||
Sequence: NYEKSDKYYYTRE | ||||||
Transmembrane | 73-97 | Helical; Name=2 | ||||
Sequence: ILGTALALARASALCLNFNSMMILI | ||||||
Topological domain | 98-130 | Cytoplasmic | ||||
Sequence: PVCRNLLSFLRGTCSFCNRTLRKPLDHNLTFHK | ||||||
Transmembrane | 131-151 | Helical; Name=3 | ||||
Sequence: LVAYMICIFTVIHIIAHLFNF | ||||||
Topological domain | 152-195 | Extracellular | ||||
Sequence: ERYRRSQQAMDGSLASVLSSLSHPEKEDSWLNPIQSPNMTVMYA | ||||||
Transmembrane | 196-216 | Helical; Name=4 | ||||
Sequence: AFTSIAGLTGVIATVALVLMV | ||||||
Topological domain | 217-234 | Cytoplasmic | ||||
Sequence: TSAMEFIRRNYFELFWYT | ||||||
Transmembrane | 235-255 | Helical; Name=5 | ||||
Sequence: HHLFIVYIICLGIHGLGGIVR | ||||||
Topological domain | 256-423 | Extracellular | ||||
Sequence: GQTEESLGESHPHNCSHSFHEWDDHKGSCRHPHFAGHPPESWKWILAPIAFYIFERILRFYRSQQKVVITKVVMHPSNVLELQMRKRGFSMEVGQYIFVNCPSISFLEWHPFTLTSAPEEEFFSVHIRAAGDWTRNLIRTFEQQHSPMPRIEVDGPFGTVSEDVFQYE | ||||||
Transmembrane | 424-444 | Helical; Name=6 | ||||
Sequence: VAVLVGAGIGVTPFASILKSI | ||||||
Topological domain | 445-591 | Cytoplasmic | ||||
Sequence: WYKFQRADNKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMEELGKMDFLNYRLFLTGWDSNIAGHAALNFDRATDILTGLKQKTSFGRPMWDNEFSRIATAHPKSAVGVFLCGPRTLAKSLRKRCQRYSSLDPRKVQFYFNKETF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000322982 | 1-591 | NADPH oxidase 1 | |||
Sequence: MAGELRGSRGPLQRIQIAPREAPNLHLTMGNWLVNHWLSVLFLVSWLGLNIFLFVYAFLNYEKSDKYYYTREILGTALALARASALCLNFNSMMILIPVCRNLLSFLRGTCSFCNRTLRKPLDHNLTFHKLVAYMICIFTVIHIIAHLFNFERYRRSQQAMDGSLASVLSSLSHPEKEDSWLNPIQSPNMTVMYAAFTSIAGLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIICLGIHGLGGIVRGQTEESLGESHPHNCSHSFHEWDDHKGSCRHPHFAGHPPESWKWILAPIAFYIFERILRFYRSQQKVVITKVVMHPSNVLELQMRKRGFSMEVGQYIFVNCPSISFLEWHPFTLTSAPEEEFFSVHIRAAGDWTRNLIRTFEQQHSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQRADNKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMEELGKMDFLNYRLFLTGWDSNIAGHAALNFDRATDILTGLKQKTSFGRPMWDNEFSRIATAHPKSAVGVFLCGPRTLAKSLRKRCQRYSSLDPRKVQFYFNKETF | ||||||
Glycosylation | 189 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 457 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylation at Thr-457 mediated by PKC/PRKBC positively regulates its interaction with NOXA1 and enzyme activity.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXO1. Interacts (via FAD-binding FR-type domain) with ARHGEF7 (via PH domain) (By similarity).
Interacts with NOXA1 (PubMed:16814099).
Interacts with NOXA1 (PubMed:16814099).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 82-316 | Ferric oxidoreductase | ||||
Sequence: RASALCLNFNSMMILIPVCRNLLSFLRGTCSFCNRTLRKPLDHNLTFHKLVAYMICIFTVIHIIAHLFNFERYRRSQQAMDGSLASVLSSLSHPEKEDSWLNPIQSPNMTVMYAAFTSIAGLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIICLGIHGLGGIVRGQTEESLGESHPHNCSHSFHEWDDHKGSCRHPHFAGHPPESWKWILAPIAFYIFERILRFY | ||||||
Domain | 317-418 | FAD-binding FR-type | ||||
Sequence: RSQQKVVITKVVMHPSNVLELQMRKRGFSMEVGQYIFVNCPSISFLEWHPFTLTSAPEEEFFSVHIRAAGDWTRNLIRTFEQQHSPMPRIEVDGPFGTVSED | ||||||
Region | 424-563 | Interaction with NOXO1 | ||||
Sequence: VAVLVGAGIGVTPFASILKSIWYKFQRADNKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMEELGKMDFLNYRLFLTGWDSNIAGHAALNFDRATDILTGLKQKTSFGRPMWDNEFSRIATAHPKSAVGVFLCGPRTL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8CIZ9-1
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
- Synonymsf-type, c-type
- NoteProduct of f-type and c-type mRNA, which differ only in 5'-UTR.
- Length591
- Mass (Da)68,193
- Last updated2010-01-19 v2
- ChecksumB2D4AE54186A066B
Q8CIZ9-2
- Name2
- Synonymsa-type
- Differences from canonical
- 1-28: Missing
Q8CIZ9-3
- Name3
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1X7 | A0A0R4J1X7_MOUSE | Nox1 | 75 | ||
E0CYB0 | E0CYB0_MOUSE | Nox1 | 526 |
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF539799 EMBL· GenBank· DDBJ | AAN75144.1 EMBL· GenBank· DDBJ | mRNA | ||
AK136432 EMBL· GenBank· DDBJ | BAE22974.1 EMBL· GenBank· DDBJ | mRNA | ||
AL671915 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AB206383 EMBL· GenBank· DDBJ | BAF03561.1 EMBL· GenBank· DDBJ | mRNA | ||
AB206384 EMBL· GenBank· DDBJ | BAF03562.1 EMBL· GenBank· DDBJ | mRNA | ||
AB206385 EMBL· GenBank· DDBJ | BAF03563.1 EMBL· GenBank· DDBJ | mRNA | ||
AY174116 EMBL· GenBank· DDBJ | AAO20852.1 EMBL· GenBank· DDBJ | mRNA |