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P80595

- APY_SOLTU

UniProt

P80595 - APY_SOLTU

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Protein

Apyrase

Gene

RROP1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates.

Catalytic activityi

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.

Cofactori

Calcium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 1701Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 5811ATP-bindingCuratedAdd
BLAST
Nucleotide bindingi194 – 20411ATP-bindingCuratedAdd
BLAST

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, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16862.

Names & Taxonomyi

Protein namesi
Recommended name:
Apyrase (EC:3.6.1.5)
Alternative name(s):
ATP-diphosphatase
ATP-diphosphohydrolase
Adenosine diphosphatase
Short name:
ADPase
Gene namesi
Name:RROP1
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454ApyrasePRO_0000019904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP80595.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Topological domaini29 – 454426ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi324 – 3296Poly-Gly

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiP80595.

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]

Sequencei

Sequence statusi: Complete.

P80595-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNQNSHFIF IILAIFLVLP LSLLSKNVNA QIPLRRHLLS HESEHYAVIF
60 70 80 90 100
DAGSTGSRVH VFRFDEKLGL LPIGNNIEYF MATEPGLSSY AEDPKAAANS
110 120 130 140 150
LEPLLDGAEG VVPQELQSET PLELGATAGL RMLKGDAAEK ILQAVRNLVK
160 170 180 190 200
NQSTFHSKDQ WVTILDGTQE GSYMWAAINY LLGNLGKDYK STTATIDLGG
210 220 230 240 250
GSVQMAYAIS NEQFAKAPQN EDGEPYVQQK HLMSKDYNLY VHSYLNYGQL
260 270 280 290 300
AGRAEIFKAS RNESNPCALE GCDGYYSYGG VDYKVKAPKK GSSWKRCRRL
310 320 330 340 350
TRHALKINAK CNIEECTFNG VWNGGGGDGQ KNIHASSFFY DIGAQVGIVD
360 370 380 390 400
TKFPSALAKP IQYLNAAKVA CQTNVADIKS IFPKTQDRNI PYLCMDLIYE
410 420 430 440 450
YTLLVDGFGL NPHKEITVIH DVQYKNYLVG AAWPLGCAID LVSSTTNKIR

VASS
Length:454
Mass (Da):50,041
Last modified:November 1, 1997 - v2
Checksum:i9D9EFE431DA2F52F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58597 mRNA. Translation: AAB02720.1.
PIRiJC4616.
UniGeneiStu.216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58597 mRNA. Translation: AAB02720.1 .
PIRi JC4616.
UniGenei Stu.216.

3D structure databases

ProteinModelPortali P80595.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

InParanoidi P80595.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16862.

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. "Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)."
    Handa M., Guidotti G.
    Biochem. Biophys. Res. Commun. 218:916-923(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-160; 236-253 AND 332-345.
    Tissue: Tuber.
  2. "Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase."
    Vasconcelos E.G., Ferreira S.T., de Carvalho T.M.U., de Souza W., Kettlun A.M., Mancilla M., Valenzuela M.A., Verjovski-Almeida S.
    J. Biol. Chem. 271:22139-22145(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-54; 68-95 AND 236-253.
    Strain: cv. Desiree.

Entry informationi

Entry nameiAPY_SOLTU
AccessioniPrimary (citable) accession number: P80595
Secondary accession number(s): Q43164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3