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O35795

- ENTP2_RAT

UniProt

O35795 - ENTP2_RAT

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Protein

Ectonucleoside triphosphate diphosphohydrolase 2

Gene

Entpd2

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

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

Isoform 1 : Cell membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2521HelicalSequence AnalysisAdd
BLAST
Topological domaini26 – 462437ExtracellularSequence AnalysisAdd
BLAST
Transmembranei463 – 48321HelicalSequence AnalysisAdd
BLAST
Topological domaini484 – 49512CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 469Combined sources
Beta strandi51 – 599Combined sources
Helixi60 – 623Combined sources
Beta strandi70 – 767Combined sources
Beta strandi78 – 803Combined sources
Helixi82 – 854Combined sources
Helixi90 – 956Combined sources
Helixi97 – 10610Combined sources
Helixi109 – 1146Combined sources
Beta strandi116 – 1216Combined sources
Helixi123 – 1319Combined sources
Helixi133 – 14715Combined sources
Beta strandi150 – 15910Combined sources
Helixi162 – 17615Combined sources
Turni177 – 1804Combined sources
Beta strandi198 – 2025Combined sources
Beta strandi204 – 2129Combined sources
Helixi220 – 2223Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi231 – 24111Combined sources
Helixi245 – 25915Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi271 – 2755Combined sources
Helixi276 – 2805Combined sources
Turni283 – 2875Combined sources
Beta strandi298 – 3036Combined sources
Helixi307 – 3159Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi342 – 3465Combined sources
Helixi347 – 35711Combined sources
Helixi366 – 37813Combined sources
Helixi381 – 3855Combined sources
Helixi395 – 3973Combined sources
Helixi398 – 41013Combined sources
Turni411 – 4133Combined sources
Helixi417 – 4204Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi427 – 4293Combined sources
Helixi437 – 4448Combined sources
Helixi453 – 4586Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35795.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
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. 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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201T → A in AAF87740. (PubMed:11229804)Curated
Sequence conflicti127 – 1282PF → LL in AAF87740. (PubMed:11229804)Curated
Sequence conflicti339 – 3391A → T in AAF87740. (PubMed:11229804)Curated
Sequence conflicti444 – 4441L → F in AAF87740. (PubMed:11229804)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei486 – 49510VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCS DLQGPGNFLSGPLERQAPEP TGWESVPCLLVKTFVIKDFS in isoform 2. 1 PublicationVSP_003613

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 .
RefSeqi NP_742027.1. NM_172030.1.
UniGenei Rn.8276.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi O35795.
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: November 26, 2014
This is version 105 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