APY4_ARATH
ID APY4_ARATH Reviewed; 503 AA.
AC Q8H1D8; B9DI02; Q94AP8; Q9XI63;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable apyrase 4;
DE Short=AtAPY4;
DE EC=3.6.1.5;
DE AltName: Full=ATP-diphosphatase;
DE AltName: Full=ATP-diphosphohydrolase;
DE AltName: Full=Adenosine diphosphatase;
DE Short=ADPase;
DE AltName: Full=NTPDase;
DE AltName: Full=Nucleoside triphosphate diphosphohydrolase 4;
GN Name=APY4; OrderedLocusNames=At1g14230; ORFNames=F7A19.33;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Yang J.;
RT "Functional analyses of Arabidopsis apyrases 3 through 7.";
RL Thesis (2011), University of Texas, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-503.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC nucleoside tri- and di-phosphates. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed both in the primary root and lateral root
CC but not in the rosette leaves. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39310.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JF830009; AEJ38085.1; -; mRNA.
DR EMBL; AC007576; AAD39310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29126.1; -; Genomic_DNA.
DR EMBL; AY045889; AAK76563.1; -; mRNA.
DR EMBL; AY150499; AAN13015.1; -; mRNA.
DR EMBL; AK317711; BAH20369.1; -; mRNA.
DR PIR; C86276; C86276.
DR RefSeq; NP_563942.1; NM_101289.5.
DR AlphaFoldDB; Q8H1D8; -.
DR SMR; Q8H1D8; -.
DR STRING; 3702.AT1G14230.1; -.
DR PaxDb; Q8H1D8; -.
DR PRIDE; Q8H1D8; -.
DR ProteomicsDB; 240885; -.
DR EnsemblPlants; AT1G14230.1; AT1G14230.1; AT1G14230.
DR GeneID; 837984; -.
DR Gramene; AT1G14230.1; AT1G14230.1; AT1G14230.
DR KEGG; ath:AT1G14230; -.
DR Araport; AT1G14230; -.
DR TAIR; locus:2035781; AT1G14230.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_5_1_1; -.
DR InParanoid; Q8H1D8; -.
DR OMA; IMGNFLE; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q8H1D8; -.
DR BioCyc; ARA:AT1G14230-MON; -.
DR BRENDA; 3.6.1.5; 399.
DR PRO; PR:Q8H1D8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1D8; baseline and differential.
DR Genevisible; Q8H1D8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..503
FT /note="Probable apyrase 4"
FT /id="PRO_0000420342"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 83..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 230..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 224
FT /note="E -> G (in Ref. 5; BAH20369)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="Q -> R (in Ref. 4; AAK76563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 55198 MW; FE9F9E3755F7FD3F CRC64;
MQRSNARSRS NINSDMVDPP EVQTSPGNHR SSPSTAAKPK SKRTKSIIFV IVACVTIALG
LLFIGYSILR SGRNRRVSLH YSVIIDGGSS GTRVHVFGYR IESGKPVFDF GEENYASLKL
SPGLSAYADN PEGVSESVTE LVEFAKKRVH KGKLKKSDIR LMATAGMRLL ELPVQEQILD
VTRRVLRSSG FDFRDEWASV ISGSDEGVYA WVVANHALGS LGGEPLKTTG IVELGGASAQ
VTFVSTELVP SEFSRTLAYG NVSYNLYSHS FLDFGQDAAQ EKLSESLYNS AANSTGEGIV
PDPCIPKGYI LETNLQKDLP GFLADKGKFT ATLQAAGNFS ECRSAAFAML QEEKGKCTYK
RCSIGSIFTP NLQGSFLATE NFFHTSKFFG LGEKEWLSEM ILAGKRFCGE EWSKLKVKYP
TFKDENLLRY CFSSAYIISM LHDSLGVALD DERIKYASKA GEEDIPLDWA LGAFILNTAT
ATFDYSGKSR KILDLSNVAK YKI
