PMA10_ARATH
ID PMA10_ARATH Reviewed; 947 AA.
AC Q43128;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATPase 10, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 10;
GN Name=AHA10; OrderedLocusNames=At1g17260; ORFNames=F20D23.4;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=7969026; DOI=10.1007/bf00282747;
RA Harper J.F., Manney L., Sussman M.R.;
RT "The plasma membrane H(+)-ATPase gene family in Arabidopsis: genomic
RT sequence of AHA10 which is expressed primarily in developing seeds.";
RL Mol. Gen. Genet. 244:572-587(1994).
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 REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: The plasma membrane H(+) ATPase of plants and fungi generates
CC a proton gradient that drives the active transport of nutrients by
CC H(+)-symport. The resulting external acidification and/or internal
CC alkinization may mediate growth responses.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Found primarily in developing seeds.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
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DR EMBL; S74033; AAB32310.2; -; Genomic_DNA.
DR EMBL; AC007651; AAD50009.3; -; Genomic_DNA.
DR EMBL; CP002684; AEE29565.1; -; Genomic_DNA.
DR PIR; S66367; S66367.
DR RefSeq; NP_173169.2; NM_101587.2.
DR AlphaFoldDB; Q43128; -.
DR SMR; Q43128; -.
DR BioGRID; 23537; 11.
DR IntAct; Q43128; 4.
DR STRING; 3702.AT1G17260.1; -.
DR iPTMnet; Q43128; -.
DR PaxDb; Q43128; -.
DR PRIDE; Q43128; -.
DR ProteomicsDB; 234677; -.
DR EnsemblPlants; AT1G17260.1; AT1G17260.1; AT1G17260.
DR GeneID; 838297; -.
DR Gramene; AT1G17260.1; AT1G17260.1; AT1G17260.
DR KEGG; ath:AT1G17260; -.
DR Araport; AT1G17260; -.
DR TAIR; locus:2020372; AT1G17260.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q43128; -.
DR OMA; FTIFGWF; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q43128; -.
DR BioCyc; ARA:AT1G17260-MON; -.
DR PRO; PR:Q43128; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q43128; baseline and differential.
DR Genevisible; Q43128; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; ISS:TAIR.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IMP:TAIR.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0010023; P:proanthocyanidin biosynthetic process; IMP:TAIR.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0007035; P:vacuolar acidification; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..947
FT /note="ATPase 10, plasma membrane-type"
FT /id="PRO_0000046283"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..89
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..299
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..672
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..677
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..700
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..758
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 813..820
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 337
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 946
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 947 AA; 104815 MW; 1E951DFCC0DA5C24 CRC64;
MAEDLDKPLL DPDTFNRKGI DLGILPLEEV FEYLRTSPQG LLSGDAEERL KIFGPNRLEE
KQENRFVKFL GFMWNPLSWV MEAAALMAIA LANSQSLGPD WEDFTGIVCL LLINATISFF
EENNAGNAAA ALMARLALKT RVLRDGQWQE QDASILVPGD IISIKLGDII PADARLLEGD
PLKIDQSVLT GESLPVTKKK GEQVFSGSTC KQGEIEAVVI ATGSTTFFGK TARLVDSTDV
TGHFQQVLTS IGNFCICSIA VGMVLEIIIM FPVQHRSYRI GINNLLVLLI GGIPIAMPTV
LSVTLAIGSH RLSQQGAITK RMTAIEEMAG MDVLCCDKTG TLTLNSLTVD KNLIEVFVDY
MDKDTILLLA GRASRLENQD AIDAAIVSML ADPREARANI REIHFLPFNP VDKRTAITYI
DSDGKWYRAT KGAPEQVLNL CQQKNEIAQR VYAIIDRFAE KGLRSLAVAY QEIPEKSNNS
PGGPWRFCGL LPLFDPPRHD SGETILRALS LGVCVKMITG DQLAIAKETG RRLGMGTNMY
PSSSLLGHNN DEHEAIPVDE LIEMADGFAG VFPEHKYEIV KILQEMKHVV GMTGDGVNDA
PALKKADIGI AVADATDAAR SSADIVLTDP GLSVIISAVL TSRAIFQRMR NYTVYAVSIT
IRIVLGFTLL ALIWEYDFPP FMVLIIAILN DGTIMTISKD RVRPSPTPES WKLNQIFATG
IVIGTYLALV TVLFYWIIVS TTFFEKHFHV KSIANNSEQV SSAMYLQVSI ISQALIFVTR
SRGWSFFERP GTLLIFAFIL AQLAATLIAV YANISFAKIT GIGWRWAGVI WLYSLIFYIP
LDVIKFVFHY ALSGEAWNLV LDRKTAFTYK KDYGKDDGSP NVTISQRSRS AEELRGSRSR
ASWIAEQTRR RAEIARLLEV HSVSRHLESV IKLKQIDQRM IRAAHTV
