ID A0A0D3AFP3_BRAOL Unreviewed; 757 AA.
AC A0A0D3AFP3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=apyrase {ECO:0000256|ARBA:ARBA00012148};
DE EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
DE AltName: Full=ATP-diphosphatase {ECO:0000256|ARBA:ARBA00031428};
DE AltName: Full=ATP-diphosphohydrolase {ECO:0000256|ARBA:ARBA00032306};
DE AltName: Full=Adenosine diphosphatase {ECO:0000256|ARBA:ARBA00030084};
DE AltName: Full=NTPDase {ECO:0000256|ARBA:ARBA00031370};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g152210.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g152210.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g152210.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000211};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR AlphaFoldDB; A0A0D3AFP3; -.
DR STRING; 109376.A0A0D3AFP3; -.
DR EnsemblPlants; Bo1g152210.1; Bo1g152210.1; Bo1g152210.
DR Gramene; Bo1g152210.1; Bo1g152210.1; Bo1g152210.
DR eggNOG; KOG0223; Eukaryota.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_368183_0_0_1; -.
DR OMA; FLWVICA; -.
DR Proteomes; UP000032141; Chromosome C1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF113; APYRASE; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 242..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 480
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 510..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 757 AA; 81032 MW; BB6A1131C4E6742B CRC64;
MLMGVIKSAI GDMLMTFSWV VLSATFGLQT TEIISAAGLH GITWAPLAIT TFLIFVYVSL
FTVVFGSASF NPTGNAAFYA AGIPGDTLFT LAIRLPAQAA GAAGGALAIM EFIPEKYKHM
ISGPSLLVDV HTGAIAETIL SFGITFAVLL IILKGPRRLL AKTLLLSLAT ICFVVAGSKY
TGPAMNPAIA FGWAYMTSSH NTWDHFYVYW ISSFVGALSA ALVFLSDSQI CDQSVSNSTR
KTIADLDPSK DPPQSVKTSA SSATTNKIRY RSPSASELLE SGLATSPTSD SDNGAKMTAK
RAIGRHDSLS EKIRRHRGLL LVISIPIVLI ALVILLMPGT TSEYALNGGG SDSKKYAVIF
DAGSSGSRVH VYCFDKNLDL VPLENELELF LQLKPGLSAY PNDPRQSANS LVTLLDKAED
SVPSELRPKT PVRVGATAGL RALGHEASEN ILQAVRELLK DRSRLKTEAN AVTVLDGTQE
GSYQWVTINY LLKTLGKPYS ETVGVVDLGG GSVQMAYAIS EKDAATAPKP LQGEDSYVRE
MYLKGRKYFL YVHSYLHYGL LAARAEILKV SEGSNNPCIV TGYDGTYKYG GTAFKAAASP
SGASVDECKR VALKALKVND SVCTHMKCTF GGVWNGGGGG GQKNMFVASF FFDRAAEAGF
VDPSQPVATV RPADFEKAAS QACNMKMGEG KTKFPRVEED NLPYLCLDLV YQYTLLVDGF
GLKPSQTITL VKKVKYGEHA VEAAWPLGSA IEAVSSL
//
