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O35795

- ENTP2_RAT

UniProt

O35795 - ENTP2_RAT

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Protein
Ectonucleoside triphosphate diphosphohydrolase 2
Gene
Entpd2, Cd39l1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Ca2+ or Mg2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Proton acceptor1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2085ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69266. Entpd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2521Helical; Reviewed prediction
Add
BLAST
Topological domaini26 – 462437Extracellular Reviewed prediction
Add
BLAST
Transmembranei463 – 48321Helical; Reviewed prediction
Add
BLAST
Topological domaini484 – 49512Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Ectonucleoside triphosphate diphosphohydrolase 2
PRO_0000209908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi75 ↔ 991 Publication
Glycosylationi129 – 1291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi242 ↔ 2841 Publication
Disulfide bondi265 ↔ 3101 Publication
Glycosylationi294 – 2941N-linked (GlcNAc...) Reviewed prediction
Glycosylationi306 – 3061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi319 – 3191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi323 ↔ 3281 Publication
Disulfide bondi377 ↔ 3991 Publication
Glycosylationi378 – 3781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi443 – 4431N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35795.
PRIDEiO35795.

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.

Gene expression databases

GenevestigatoriO35795.

Interactioni

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 469
Beta strandi51 – 599
Helixi60 – 623
Beta strandi70 – 767
Beta strandi78 – 803
Helixi82 – 854
Helixi90 – 956
Helixi97 – 10610
Helixi109 – 1146
Beta strandi116 – 1216
Helixi123 – 1319
Helixi133 – 14715
Beta strandi150 – 15910
Helixi162 – 17615
Turni177 – 1804
Beta strandi198 – 2025
Beta strandi204 – 2129
Helixi220 – 2223
Beta strandi223 – 2286
Beta strandi231 – 24111
Helixi245 – 25915
Beta strandi261 – 2633
Beta strandi271 – 2755
Helixi276 – 2805
Turni283 – 2875
Beta strandi298 – 3036
Helixi307 – 3159
Beta strandi324 – 3307
Beta strandi342 – 3465
Helixi347 – 35711
Helixi366 – 37813
Helixi381 – 3855
Helixi395 – 3973
Helixi398 – 41013
Turni411 – 4133
Helixi417 – 4204
Beta strandi423 – 4253
Beta strandi427 – 4293
Helixi437 – 4448
Helixi453 – 4586

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4CD1X-ray2.00A28-462[»]
4CD3X-ray2.19A28-461[»]
ProteinModelPortaliO35795.
SMRiO35795. Positions 36-461.

Miscellaneous databases

EvolutionaryTraceiO35795.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
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. Align

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

MAGKLVSLVP PLLLAAAGLT GLLLLCVPTQ DVREPPALKY GIVLDAGSSH    50
TSMFVYKWPA DKENDTGIVG QHSSCDVQGG GISSYANDPS KAGQSLVRCL 100
EQALRDVPRD RHASTPLYLG ATAGMRPFNL TSPEATARVL EAVTQTLTQY 150
PFDFRGARIL SGQDEGVFGW VTANYLLENF IKYGWVGRWI RPRKGTLGAM 200
DLGGASTQIT FETTSPSEDP GNEVHLRLYG QHYRVYTHSF LCYGRDQILL 250
RLLASALQIH RFHPCWPKGY STQVLLQEVY QSPCTMGQRP RAFNGSAIVS 300
LSGTSNATLC RDLVSRLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY 350
TVDFLTTVMG LPVGTLKQLE EATEITCNQT WTELQARVPG QKTRLADYCA 400
VAMFIHQLLS RGYHFDERSF REVVFQKKAA DTAVGWALGY MLNLTNLIPA 450
DLPGLRKGTH FSSWVALLLL FTVLILAALV LLLRQVRSAK SPGAL 495
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei486 – 49510VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCS DLQGPGNFLSGPLERQAPEP TGWESVPCLLVKTFVIKDFS in isoform 2.
VSP_003613

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201T → A in AAF87740. 1 Publication
Sequence conflicti127 – 1282PF → LL in AAF87740. 1 Publication
Sequence conflicti339 – 3391A → T in AAF87740. 1 Publication
Sequence conflicti444 – 4441L → F in AAF87740. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Y11835 mRNA. Translation: CAA72533.1 .
AF276940 mRNA. Translation: AAF87740.1 .
AF129103 mRNA. Translation: AAD42303.1 .
RefSeqi NP_742027.1. NM_172030.1.
UniGenei Rn.8276.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CJ1 X-ray 1.70 A 29-461 [» ]
3CJ7 X-ray 1.80 A 29-461 [» ]
3CJ9 X-ray 1.80 A 29-461 [» ]
3CJA X-ray 2.10 A 29-461 [» ]
4BQZ X-ray 2.05 A 28-462 [» ]
4BR0 X-ray 2.05 A 28-462 [» ]
4BR2 X-ray 2.00 A 28-462 [» ]
4CD1 X-ray 2.00 A 28-462 [» ]
4CD3 X-ray 2.19 A 28-461 [» ]
ProteinModelPortali O35795.
SMRi O35795. Positions 36-461.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O35795.
ChEMBLi CHEMBL3300.

Proteomic databases

PaxDbi O35795.
PRIDEi O35795.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64467.
KEGGi rno:64467.
UCSCi RGD:69266. rat. [O35795-1 ]

Organism-specific databases

CTDi 954.
RGDi 69266. Entpd2.

Phylogenomic databases

eggNOGi COG5371.
HOGENOMi HOG000059572.
HOVERGENi HBG018982.
KOi K01509.
PhylomeDBi O35795.

Miscellaneous databases

EvolutionaryTracei O35795.
NextBioi 613232.
PROi O35795.

Gene expression databases

Genevestigatori O35795.

Family and domain databases

InterProi IPR000407. GDA1_CD39_NTPase.
[Graphical view ]
PANTHERi PTHR11782. PTHR11782. 1 hit.
Pfami PF01150. GDA1_CD39. 1 hit.
[Graphical view ]
PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain."
    Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.
    Neuropharmacology 36:1189-1200(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Ecto-ATPase mRNA is regulated by FSH in Sertoli cells."
    Lu Q., Porter L.D., Cui X., Sanborn B.M.
    J. Androl. 22:289-301(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Sertoli cell.
  3. "Evidence for alternative splicing of ecto-ATPase associated with termination of purinergic transmission."
    Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.
    Brain Res. Mol. Brain Res. 73:85-92(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-495 (ISOFORM 2).
    Strain: Wistar.
    Tissue: Cochlea.
  4. "Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling."
    Zebisch M., Strater N.
    Proc. Natl. Acad. Sci. U.S.A. 105:6882-6887(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-461 ALONE AND IN COMPLEX WITH ATP ANALOGS AND CALCIUM, ACTIVE SITE, DISULFIDE BONDS.

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: May 14, 2014
This is version 102 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

External Data

Dasty 3

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