O55026 · ENTP2_MOUSE
- ProteinEctonucleoside triphosphate diphosphohydrolase 2
- GeneEntpd2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids495 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity).
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basement membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | nucleoside diphosphate phosphatase activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | platelet activation | |
Biological Process | purine ribonucleoside diphosphate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEctonucleoside triphosphate diphosphohydrolase 2
- EC number
- Short namesNTPDase 2
- Alternative names
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 accessionO55026
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform Long
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MAGK | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: LVSLVPPLLLAAVGLAGLLLL | ||||||
Topological domain | 26-462 | Extracellular | ||||
Sequence: CVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFS | ||||||
Transmembrane | 463-483 | Helical | ||||
Sequence: SWVALLLLFTVLILAALVLLL | ||||||
Topological domain | 484-495 | Cytoplasmic | ||||
Sequence: RQVRSAKSPGAL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000209907 | 1-495 | Ectonucleoside triphosphate diphosphohydrolase 2 | |||
Sequence: MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 75↔99 | |||||
Sequence: CDVRGGGISSYANDPSRAGQSLVEC | ||||||
Glycosylation | 129 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 242↔284 | |||||
Sequence: CYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPC | ||||||
Disulfide bond | 265↔310 | |||||
Sequence: CWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALC | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 319 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 323↔328 | |||||
Sequence: CPFSQC | ||||||
Disulfide bond | 377↔399 | |||||
Sequence: CNQTWAELQARVPGQQTRLPDYC | ||||||
Glycosylation | 378 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 443 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O55026-1
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.
- NameLong
- Length495
- Mass (Da)54,319
- Last updated2004-03-15 v2
- ChecksumA76468A0CBF86AAC
O55026-2
- NameShort
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_003611 | 130-132 | in isoform Short | |||
Sequence: LTS → MAG | ||||||
Alternative sequence | VSP_003612 | 133-495 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 400 | in Ref. 2; AAC24347 | ||||
Sequence: A → T | ||||||
Sequence conflict | 414 | in Ref. 2; AAC24347 | ||||
Sequence: R → S | ||||||
Sequence conflict | 437 | in Ref. 2; AAC24347 | ||||
Sequence: A → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U91511 EMBL· GenBank· DDBJ | AAB81014.1 EMBL· GenBank· DDBJ | mRNA | ||
AF042811 EMBL· GenBank· DDBJ | AAC24347.1 EMBL· GenBank· DDBJ | mRNA | ||
AY376711 EMBL· GenBank· DDBJ | AAQ86586.1 EMBL· GenBank· DDBJ | mRNA | ||
AK002553 EMBL· GenBank· DDBJ | BAB22182.1 EMBL· GenBank· DDBJ | mRNA |