[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. STRAIN=Beverley, and RH; DOI=10.1074/jbc.270.19.11391; PubMed=7744775 [NCBI, ExPASy, EBI, Israel, Japan] Asai T., Miura S., Sibley L.D., Okabayashi H., Takeuchi T.; "Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii."; J. Biol. Chem. 270:11391-11397(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=RH; PubMed=7961894 [NCBI, ExPASy, EBI, Israel, Japan] Bermudes D., Peck K.R., Afifi M.A., Beckers C.J.M., Joiner K.A.; "Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii."; J. Biol. Chem. 269:29252-29260(1994).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-523. STRAIN=RH; DOI=10.1016/0378-1119(89)90484-8; PubMed=2482826 [NCBI, ExPASy, EBI, Israel, Japan] Johnson A.M., Illana S., McDonald P.J., Asai T.; "Cloning, expression and nucleotide sequence of the gene fragment encoding an antigenic portion of the nucleoside triphosphate hydrolase of Toxoplasma gondii."; Gene 85:215-220(1989).

Comments

FUNCTION: May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite. NTPAse-II has a specific activity 4.5-fold lower than NTPAse-I in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
CATALYTIC ACTIVITY: NTP + H₂O = NDP + phosphate.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Secreted. Parasitophorous vacuole. Note=Found in host cell parasitophorous vacuole.
SIMILARITY: Belongs to the GDA1/CD39 NTPase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L39077; AAC41569.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L39079; AAC41570.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U96965; AAC80187.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33472; AAA30143.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55421; A55421.

3D structure databases

ModBase

Q27895.

Ontologies

GO:0020003;	Cellular component: parasitophorous vacuole (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR000407; GDA1_CD39_NTPase.
IPR017227; NTPase.
Graphical view of domain structure.

PANTHER

PTHR11782; GDA1_CD39_NTPase; 1.

Pfam

PF01150; GDA1_CD39; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037506; NTPase; 1.

PROSITE

PS01238; GDA1_CD39_NTPASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Signal; Vacuole.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`
`CHAIN`	`26 628`	`603`	`Nucleoside-triphosphatase 2.`	`PRO_0000019912`
`CARBOHYD`	`432 432`		`N-linked (GlcNAc...) (Potential).`
`VARIANT`	`6 6`	`1`	`Y -> H (in strain: Beverley).`
`VARIANT`	`91 91`	`1`	`K -> R (in strain: Beverley).`
`VARIANT`	`101 101`	`1`	`Q -> R (in strain: Beverley).`
`CONFLICT`	`334 334`		`G -> R (in Ref. 3; AAA30143).`
`CONFLICT`	`370 370`		`V -> L (in Ref. 3).`
`CONFLICT`	`372 372`		`V -> L (in Ref. 3).`
`CONFLICT`	`399 399`		`H -> N (in Ref. 3; AAA30143).`
`CONFLICT`	`437 437`		`E -> K (in Ref. 3; AAA30143).`
`CONFLICT`	`488 489`		`FI -> IV (in Ref. 3).`
`CONFLICT`	`492 494`		`REM -> GGS (in Ref. 3).`
`CONFLICT`	`497 497`		`S -> A (in Ref. 3).`
`CONFLICT`	`499 499`		`D -> N (in Ref. 3).`
`CONFLICT`	`523 523`		`R -> G (in Ref. 3; AAA30143).`

Sequence information

Length: 628 AA [This is the length of the unprocessed precursor]

Molecular weight: 69585 Da [This is the MW of the unprocessed precursor]

CRC64: DE943DFDAC641159 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWLPVYVPLL LVFGVSLSLP HGSLGTDSSS LRGVDADTEK RINVGKTHLQ TLRNLETRCH 

        70         80         90        100        110        120 
DSLQALVVID AGSSSTRTNV FLAKTRSCPN KGRSIDPDSI QLIREGKRFT GLRVVLEEWL 

       130        140        150        160        170        180 
DTYAGKDWES RPVDARLLFQ YVPQMHEGAK KLMQLLEEDT VAILDSQLNE EQKVQVKALG 

       190        200        210        220        230        240 
IPVMLCSTAG VRDFHEWYRD ALFVLLRHLI NNPSPAHGYK FFTNPFWTRP ITGAEEGLFA 

       250        260        270        280        290        300 
FITLNHLSRR LGEDPARCMI DEYGVKHCRN DLAGVVEVGG ASAQIVFPLQ EGTVLPSSVR 

       310        320        330        340        350        360 
AVNLQRERLL PERYPSADVV SVSFMQLGMA SSAGLFLKEL CSNDEFLQGG ICSNPCLFKG 

       370        380        390        400        410        420 
FQQSCSAGEV EVRPDGSASV NEDVRKNRLK PLATYCSVHN PEISFKVTNE MQCRENSIDP 

       430        440        450        460        470        480 
TKPLAERMKI ENCSIIEGTG NFDKCVSQVE SILVAPKLPL PANIEAASSG FESVDQVFRF 

       490        500        510        520        530        540 
ASSTAPMFIT GREMLASIDT LKDHRLLRSD FSGDVEELAE AAREFCSSEV IIRTDGPVIQ 

       550        560        570        580        590        600 
LPNARGEQKL NSLNFDLCKT MALTVSLLRH MAAGENQPSF IKWEKSIAGP DGKPLADLGW 

       610        620 
QVGVILHHVL FTEEWGRTAY EAGYSHNL

Q27895 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools