Reviewed, UniProtKB/Swiss-Prot P50635 (APY_AEDAE)

Names and origin

Protein names

Recommended name:
    Apyrase
    EC=3.6.1.5
Alternative name(s):
    Adenosine diphosphatase
    ATP-diphosphohydrolase
    ATP-diphosphatase
      Short name=ADPase
    Allergen=Aed a 1

Gene names

Name:	APY
ORF Names:	AAEL006347

Organism

Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [Complete proteome]

Taxonomic identifier

7159 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Culicini › Aedes › Stegomyia

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Facilitates hematophagy by preventing ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood.
Catalytic activity	ATP + 2 H2O = AMP + 2 phosphate.
Cofactor	Divalent cations By similarity.
Subcellular location	Secreted.
Tissue specificity	Salivary gland specific.
Developmental stage	Not detectable in females on the first day after eclosion, but is detectable on the second day. It is maximally expressed by day 4.
Post-translational modification	The N-terminus is blocked.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Ligand	ATP-binding Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 562	538	Apyrase		PRO_0000000039
Regions
	Region	508 – 514	7	Substrate binding By similarity
Sites
	Metal binding	47	1	Divalent metal cation 1 By similarity
	Metal binding	49	1	Divalent metal cation 1 By similarity
	Metal binding	98	1	Divalent metal cation 1 By similarity
	Metal binding	98	1	Divalent metal cation 2 By similarity
	Metal binding	130	1	Divalent metal cation 2 By similarity
	Metal binding	233	1	Divalent metal cation 2 By similarity
	Metal binding	257	1	Divalent metal cation 2 By similarity
	Binding site	424	1	Substrate By similarity
	Site	131	1	Transition state stabilizer By similarity
	Site	134	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	390	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	9	1	E → A in strain: Rockefeller.
	Natural variant	30	1	V → P in strain: Rockefeller.
	Natural variant	61	1	V → A in strain: Rockefeller.
	Natural variant	224	1	N → K in strain: Rockefeller.
	Natural variant	284	1	L → I in strain: Rockefeller.
	Natural variant	314 – 315	2	EE → DT in strain: Rockefeller.
	Natural variant	319 – 320	2	KN → QH in strain: Rockefeller.
	Natural variant	347	1	A → E in strain: Rockefeller.
	Natural variant	361	1	M → K in strain: Rockefeller.
	Natural variant	472	1	V → I in strain: Rockefeller.
	Natural variant	491	1	K → E in strain: Rockefeller.
	Natural variant	498	1	E → Q in strain: Rockefeller.
Experimental info
	Sequence conflict	30	1	V → A in AAA99189. Ref.2
	Sequence conflict	358	1	G → GG in AAA99189. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P50635-1 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: EEC3C6BE34235EFD	FASTA	562	62,754
	10 20 30 40 50 60 MAGRPGYSEV IFLYVVSVAV IARATDNMPV NKDVSKLFPL TLIHINDLHA RFEETNMKSN 70 80 90 100 110 120 VCTQKDQCIA GIARVYQKIK DLLKEYESKN PIYLNAGDNF QGTLWYNLLR WNVTADFIKK 130 140 150 160 170 180 LKPAAMTLGN HEFDHTPKGL APYLAELNKE GIPTIVANLV MNNDPDLKSS KIPKSIKLTV 190 200 210 220 230 240 GKRKIGIIGV LYDKTHEIAQ TGKVTLSNAV EAVRREAAAL KKDNIDIIVV LSHCSYEEDK 250 260 270 280 290 300 KIAAEAGDDI DVIVGAHSHS FLYSPDSKQP HDPKDKVEGP YPTLVESKNK RKIPIVQAKS 310 320 330 340 350 360 FGKYVGRLTL YFDEEGEVKN WEGYPVFIDH KVQQDPQILK DLVPWRAKVE AIGSTVVGET 370 380 390 400 410 420 MIELDRDSCR DQECTLGVLY ADGFADQYTN DTFRPFAIIQ AGNFRNPIKV GKITNGDIIE 430 440 450 460 470 480 AAPFGSTADL IRLKGADIWD VAEHSFALDD EGRTNCLQVS GLRIVIDISK PVRSRVKKIE 490 500 510 520 530 540 VMDYTNPKSD KLKPLDKEAE YYIVVPSYLA DGKDGFSAMK RATARRTGPL DSDVFKNYVE 550 560 KIKKVDNLKL GRVIVCKGSK CT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family." Champagne D.E., Smartt C.T., Ribeiro J.M.C., James A.A. Proc. Natl. Acad. Sci. U.S.A. 92:694-698(1995) [PubMed: 7846038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 308-331 AND 498-521. Strain: Rockefeller. Tissue: Salivary gland.
[2]	"The apyrase gene of the vector mosquito, Aedes aegypti, is expressed specifically in the adult female salivary glands." Smartt C.T., Kim A.P., Grossman G.L., James A.A. Exp. Parasitol. 81:239-248(1995) [PubMed: 7498420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Rockefeller. Tissue: Salivary gland.
[3]	"Genome sequence of Aedes aegypti, a major arbovirus vector." Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P. , Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W. Science 316:1718-1723(2007) [PubMed: 17510324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Liverpool.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L12389 mRNA. Translation: AAC37218.1. L41391 Genomic DNA. Translation: AAA99189.1. CH477386 Genomic DNA. Translation: EAT42070.1.
RefSeq	XP_001651910.1.
UniGene	Aae.5859
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	AAEL006347-RA; AAEL006347-PA; AAEL006347; Aedes aegypti. [Genome view]
GeneID	5567877.
KEGG	aag:AaeL_AAEL006347.
VectorBase	AAEL006347. Aedes aegypti.
Phylogenomic databases
OMA	TLIHIND.
Enzyme and pathway databases
BRENDA	3.6.1.5. 1026.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APY_AEDAE

Accession

Primary (citable) accession number: P50635
Secondary accession number(s): Q176L2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 1, 2008
Last modified:	November 3, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)