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Protein

Ectonucleoside triphosphate diphosphohydrolase 2

Gene

Entpd2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Proton acceptorBy similarity

Regions

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

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: Ensembl
  • ATPase activity Source: Ensembl
  • ATP binding Source: UniProtKB-KW
  • nucleoside-diphosphatase activity Source: MGI
  • nucleoside-triphosphatase activity Source: MGI

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1096863. Entpd2.

Subcellular locationi

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

  • basal lamina Source: MGI
  • cell body Source: Ensembl
  • cell projection membrane Source: Ensembl
  • cell surface Source: Ensembl
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Ectonucleoside triphosphate diphosphohydrolase 2PRO_0000209907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi75 ↔ 99By similarity
Glycosylationi129 – 1291N-linked (GlcNAc...)1 Publication
Disulfide bondi242 ↔ 284By similarity
Disulfide bondi265 ↔ 310By similarity
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi323 ↔ 328By similarity
Disulfide bondi377 ↔ 399By similarity
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO55026.
PRIDEiO55026.

Expressioni

Inductioni

By dioxin.

Gene expression databases

BgeeiO55026.
ExpressionAtlasiO55026. baseline and differential.
GenevisibleiO55026. MM.

Interactioni

Protein-protein interaction databases

IntActiO55026. 1 interaction.
STRINGi10090.ENSMUSP00000028328.

Structurei

3D structure databases

ProteinModelPortaliO55026.
SMRiO55026. Positions 36-461.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiO55026.
KOiK01509.
OMAiSPCTMAQ.
OrthoDBiEOG754HPX.
PhylomeDBiO55026.
TreeFamiTF332859.

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 Long (identifier: O55026-1) [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 PLLLAAVGLA GLLLLCVPTQ DVREPPALKY GIVLDAGSSH
60 70 80 90 100
TSMFVYKWPA DKENDTGIVG QHSSCDVRGG GISSYANDPS RAGQSLVECL
110 120 130 140 150
EQALRDVPKD RYASTPLYLG ATAGMRLLNL TSPEATAKVL EAVTQTLTRY
160 170 180 190 200
PFDFRGARIL SGQDEGVFGW VTANYLLENF IKYGWVGRWI RPRKGTLGAM
210 220 230 240 250
DLGGASTQIT FETTSPSEDP DNEVHLRLYG QHYRVYTHSF LCYGRDQVLQ
260 270 280 290 300
RLLASALQIH RFHPCWPKGY STQVLLREVY QSPCTMGQRP QTFNSSATVS
310 320 330 340 350
LSGTSNAALC RDLVSGLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY
360 370 380 390 400
TVDFLKTVMG LPVGTLKQLE DATETTCNQT WAELQARVPG QQTRLPDYCA
410 420 430 440 450
VAMFIHQLLS RGYRFDERSF RGVVFEKKAA DTAVGWALGY MLNLTNLIPA
460 470 480 490
DLPGLRKGTH FSSWVALLLL FTVLILAALV LLLRQVRSAK SPGAL
Length:495
Mass (Da):54,319
Last modified:March 15, 2004 - v2
Checksum:iA76468A0CBF86AAC
GO
Isoform Short (identifier: O55026-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     130-132: LTS → MAG
     133-495: Missing.

Show »
Length:132
Mass (Da):13,857
Checksum:i12D83F5F057F6A7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti400 – 4001A → T in AAC24347 (PubMed:9624117).Curated
Sequence conflicti414 – 4141R → S in AAC24347 (PubMed:9624117).Curated
Sequence conflicti437 – 4371A → T in AAC24347 (PubMed:9624117).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 1323LTS → MAG in isoform Short. 1 PublicationVSP_003611
Alternative sequencei133 – 495363Missing in isoform Short. 1 PublicationVSP_003612Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91511 mRNA. Translation: AAB81014.1.
AF042811 mRNA. Translation: AAC24347.1.
AY376711 mRNA. Translation: AAQ86586.1.
AK002553 mRNA. Translation: BAB22182.1.
CCDSiCCDS15770.1. [O55026-1]
RefSeqiNP_033979.2. NM_009849.2. [O55026-1]
UniGeneiMm.482100.

Genome annotation databases

EnsembliENSMUST00000028328; ENSMUSP00000028328; ENSMUSG00000015085. [O55026-1]
GeneIDi12496.
KEGGimmu:12496.
UCSCiuc008irw.2. mouse. [O55026-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91511 mRNA. Translation: AAB81014.1.
AF042811 mRNA. Translation: AAC24347.1.
AY376711 mRNA. Translation: AAQ86586.1.
AK002553 mRNA. Translation: BAB22182.1.
CCDSiCCDS15770.1. [O55026-1]
RefSeqiNP_033979.2. NM_009849.2. [O55026-1]
UniGeneiMm.482100.

3D structure databases

ProteinModelPortaliO55026.
SMRiO55026. Positions 36-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO55026. 1 interaction.
STRINGi10090.ENSMUSP00000028328.

Proteomic databases

PaxDbiO55026.
PRIDEiO55026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028328; ENSMUSP00000028328; ENSMUSG00000015085. [O55026-1]
GeneIDi12496.
KEGGimmu:12496.
UCSCiuc008irw.2. mouse. [O55026-1]

Organism-specific databases

CTDi954.
MGIiMGI:1096863. Entpd2.

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiO55026.
KOiK01509.
OMAiSPCTMAQ.
OrthoDBiEOG754HPX.
PhylomeDBiO55026.
TreeFamiTF332859.

Miscellaneous databases

PROiO55026.
SOURCEiSearch...

Gene expression databases

BgeeiO55026.
ExpressionAtlasiO55026. baseline and differential.
GenevisibleiO55026. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes."
    Chadwick B.P., Frischauf A.-M.
    Mamm. Genome 8:668-672(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Tissue: Embryo.
  2. "A novel response to dioxin. Induction of ecto-ATPase gene expression."
    Gao L., Dong L., Whitlock J.P. Jr.
    J. Biol. Chem. 273:15358-15365(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Hepatoma.
  3. "Cloning of mouse heart nucleoside triphosphate diphosphohydrolase-2."
    Lavoie E.G., Lecka J., Sevigny J.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Strain: CD-1.
    Tissue: Heart.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Strain: C57BL/6J.
    Tissue: Kidney.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-129.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung, Pancreas and Testis.

Entry informationi

Entry nameiENTP2_MOUSE
AccessioniPrimary (citable) accession number: O55026
Secondary accession number(s): O35928, Q9DCR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: March 15, 2004
Last modified: June 8, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.