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Protein

Ectonucleoside triphosphate diphosphohydrolase 2

Gene

Entpd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei165Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi204 – 208ATP5

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: RGD
  • ATPase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: RGD

GO - Biological processi

  • cellular response to interferon-alpha Source: RGD
  • cellular response to interleukin-6 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • protein homooligomerization Source: RGD
  • response to auditory stimulus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.1.5. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleoside triphosphate diphosphohydrolase 2 (EC:3.6.1.-)
Short name:
NTPDase 2
Alternative name(s):
CD39 antigen-like 1
Ecto-ATP diphosphohydrolase 2
Short name:
Ecto-ATPDase 2
Short name:
Ecto-ATPase 2
Gene namesi
Name:Entpd2
Synonyms:Cd39l1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69266. Entpd2.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 25HelicalSequence analysisAdd BLAST21
Topological domaini26 – 462ExtracellularSequence analysisAdd BLAST437
Transmembranei463 – 483HelicalSequence analysisAdd BLAST21
Topological domaini484 – 495CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • cell body Source: RGD
  • cell projection membrane Source: RGD
  • cell surface Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002099081 – 495Ectonucleoside triphosphate diphosphohydrolase 2Add BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi64N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi75 ↔ 991 Publication
Glycosylationi129N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi242 ↔ 2841 Publication
Disulfide bondi265 ↔ 3101 Publication
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi306N-linked (GlcNAc...)Sequence analysis1
Glycosylationi319N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi323 ↔ 3281 Publication
Disulfide bondi377 ↔ 3991 Publication
Glycosylationi378N-linked (GlcNAc...)Sequence analysis1
Glycosylationi443N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35795.
PRIDEiO35795.

PTM databases

iPTMnetiO35795.
PhosphoSitePlusiO35795.
UniCarbKBiO35795.

Expressioni

Tissue specificityi

Expressed in brain, heart, vas deferens, kidney, skeletal muscle, thymus, lung and spleen. Weak expression in liver.

Inductioni

By FSH in Sertoli cells but not in peritubular cells; by cAMP in both type of cells.

Interactioni

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017829.

Chemistry databases

BindingDBiO35795.

Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 46Combined sources9
Beta strandi51 – 59Combined sources9
Helixi60 – 62Combined sources3
Beta strandi70 – 76Combined sources7
Beta strandi78 – 80Combined sources3
Helixi82 – 85Combined sources4
Helixi90 – 95Combined sources6
Helixi97 – 106Combined sources10
Helixi109 – 114Combined sources6
Beta strandi116 – 121Combined sources6
Helixi123 – 131Combined sources9
Helixi133 – 147Combined sources15
Beta strandi150 – 159Combined sources10
Helixi162 – 176Combined sources15
Turni177 – 180Combined sources4
Beta strandi198 – 202Combined sources5
Beta strandi204 – 212Combined sources9
Helixi220 – 222Combined sources3
Beta strandi223 – 228Combined sources6
Beta strandi231 – 241Combined sources11
Helixi245 – 259Combined sources15
Beta strandi261 – 263Combined sources3
Beta strandi271 – 275Combined sources5
Helixi276 – 280Combined sources5
Turni283 – 287Combined sources5
Beta strandi298 – 303Combined sources6
Helixi307 – 315Combined sources9
Beta strandi324 – 330Combined sources7
Beta strandi342 – 346Combined sources5
Helixi347 – 357Combined sources11
Helixi366 – 378Combined sources13
Helixi381 – 385Combined sources5
Helixi395 – 397Combined sources3
Helixi398 – 410Combined sources13
Turni411 – 413Combined sources3
Helixi417 – 420Combined sources4
Beta strandi423 – 425Combined sources3
Beta strandi427 – 429Combined sources3
Helixi437 – 444Combined sources8
Helixi453 – 458Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CJ1X-ray1.70A29-461[»]
3CJ7X-ray1.80A29-461[»]
3CJ9X-ray1.80A29-461[»]
3CJAX-ray2.10A29-461[»]
4BQZX-ray2.05A28-462[»]
4BR0X-ray2.05A28-462[»]
4BR2X-ray2.00A28-462[»]
4BR5X-ray1.75A28-462[»]
4CD1X-ray2.00A28-462[»]
4CD3X-ray2.19A28-461[»]
ProteinModelPortaliO35795.
SMRiO35795.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35795.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiO35795.
KOiK01509.
PhylomeDBiO35795.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35795-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGKLVSLVP PLLLAAAGLT GLLLLCVPTQ DVREPPALKY GIVLDAGSSH
60 70 80 90 100
TSMFVYKWPA DKENDTGIVG QHSSCDVQGG GISSYANDPS KAGQSLVRCL
110 120 130 140 150
EQALRDVPRD RHASTPLYLG ATAGMRPFNL TSPEATARVL EAVTQTLTQY
160 170 180 190 200
PFDFRGARIL SGQDEGVFGW VTANYLLENF IKYGWVGRWI RPRKGTLGAM
210 220 230 240 250
DLGGASTQIT FETTSPSEDP GNEVHLRLYG QHYRVYTHSF LCYGRDQILL
260 270 280 290 300
RLLASALQIH RFHPCWPKGY STQVLLQEVY QSPCTMGQRP RAFNGSAIVS
310 320 330 340 350
LSGTSNATLC RDLVSRLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY
360 370 380 390 400
TVDFLTTVMG LPVGTLKQLE EATEITCNQT WTELQARVPG QKTRLADYCA
410 420 430 440 450
VAMFIHQLLS RGYHFDERSF REVVFQKKAA DTAVGWALGY MLNLTNLIPA
460 470 480 490
DLPGLRKGTH FSSWVALLLL FTVLILAALV LLLRQVRSAK SPGAL
Length:495
Mass (Da):54,390
Last modified:January 1, 1998 - v1
Checksum:i237B999F1BEB8E00
GO
Isoform 2 (identifier: O35795-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     486-495: VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCSDLQGPGNFLSGPLERQAPEPTGWESVPCLLVKTFVIKDFS

Show »
Length:545
Mass (Da):60,067
Checksum:i9802C097CA40E93C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20T → A in AAF87740 (PubMed:11229804).Curated1
Sequence conflicti127 – 128PF → LL in AAF87740 (PubMed:11229804).Curated2
Sequence conflicti339A → T in AAF87740 (PubMed:11229804).Curated1
Sequence conflicti444L → F in AAF87740 (PubMed:11229804).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003613486 – 495VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCS DLQGPGNFLSGPLERQAPEP TGWESVPCLLVKTFVIKDFS in isoform 2. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11835 mRNA. Translation: CAA72533.1.
AF276940 mRNA. Translation: AAF87740.1.
AF129103 mRNA. Translation: AAD42303.1.
RefSeqiNP_742027.1. NM_172030.1.
UniGeneiRn.8276.

Genome annotation databases

GeneIDi64467.
KEGGirno:64467.
UCSCiRGD:69266. rat. [O35795-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11835 mRNA. Translation: CAA72533.1.
AF276940 mRNA. Translation: AAF87740.1.
AF129103 mRNA. Translation: AAD42303.1.
RefSeqiNP_742027.1. NM_172030.1.
UniGeneiRn.8276.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CJ1X-ray1.70A29-461[»]
3CJ7X-ray1.80A29-461[»]
3CJ9X-ray1.80A29-461[»]
3CJAX-ray2.10A29-461[»]
4BQZX-ray2.05A28-462[»]
4BR0X-ray2.05A28-462[»]
4BR2X-ray2.00A28-462[»]
4BR5X-ray1.75A28-462[»]
4CD1X-ray2.00A28-462[»]
4CD3X-ray2.19A28-461[»]
ProteinModelPortaliO35795.
SMRiO35795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017829.

Chemistry databases

BindingDBiO35795.
ChEMBLiCHEMBL3300.

PTM databases

iPTMnetiO35795.
PhosphoSitePlusiO35795.
UniCarbKBiO35795.

Proteomic databases

PaxDbiO35795.
PRIDEiO35795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64467.
KEGGirno:64467.
UCSCiRGD:69266. rat. [O35795-1]

Organism-specific databases

CTDi954.
RGDi69266. Entpd2.

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiO35795.
KOiK01509.
PhylomeDBiO35795.

Enzyme and pathway databases

BRENDAi3.6.1.5. 5301.

Miscellaneous databases

EvolutionaryTraceiO35795.
PROiO35795.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENTP2_RAT
AccessioniPrimary (citable) accession number: O35795
Secondary accession number(s): Q9JHY5, Q9WVE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.