(data stored in ACNUC7421 zone)

HOGENOM: ARATH_4_PE3920

ID   ARATH_4_PE3920                       STANDARD;      PRT;   948 AA.
AC   ARATH_4_PE3920; P19456;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATPase 2, plasma membrane-type; EC=3.6.3 6;AltName:
DE   Full=Proton pump 2; (ARATH_4.PE3920).
GN   Name=AHA2; OrderedLocusNames=At4g30190; ORFNames=F9N11.40;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_4.PE3920.
CC       Arabidopsis thaliana chromosome 4 TAIR10 full sequence 1..18585056
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PMA2_ARATH
CC   -!- FUNCTION: The plasma membrane H(+) ATPase of plants and fungi
CC       generates a proton gradient that drives the active transport of
CC       nutrients by H(+)-symport. The resulting external acidification
CC       and/or internal alkinization may mediate growth responses.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: Binds to 14-3-3 proteins. The binding is induced by
CC       phosphorylation of Thr-947. Binding to 14-3-3 proteins activates
CC       the H(+)-ATPase.
CC   -!- INTERACTION:
CC       O22932:CIPK11; NbExp=3; IntAct=EBI-2293350, EBI-537638;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences;
CC       Name=1;
CC         IsoId=P19456-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Higher levels in roots than in shoots.
CC   -!- PTM: Phosphorylation level varies significantly during early
CC       response to general elicitors.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIIA subfamily.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT4G30190;AT4G30190.1;AT4G30190.1.
DR   EMBL; AK318876; - ;
DR   EMBL; AL109796; - ;
DR   EMBL; AL161576; - ;
DR   EMBL; AY035075; - ;
DR   EMBL; BT000781; - ;
DR   EMBL; BT001969; - ;
DR   EMBL; J05570; - ;
DR   UniProtKB/Swiss-Prot; P19456; -.
DR   EMBL; J05570; AAA32751.1; -; Genomic_DNA.
DR   EMBL; AL109796; CAB52463.1; -; Genomic_DNA.
DR   EMBL; AL161576; CAB81012.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85731.1; -; Genomic_DNA.
DR   EMBL; AY035075; AAK59580.1; -; mRNA.
DR   EMBL; BT000781; AAN31920.1; -; mRNA.
DR   EMBL; BT001969; AAN71968.1; -; mRNA.
DR   IPI; IPI00529487; -.
DR   PIR; A37116; PXMUP2.
DR   RefSeq; NP_194748.1; NM_119165.3.
DR   UniGene; At.23014; -.
DR   PDB; 3B8C; X-ray; 3.60 A; A/B=1-875.
DR   PDBsum; 3B8C; -.
DR   ProteinModelPortal; P19456; -.
DR   SMR; P19456; 12-844, 900-942.
DR   IntAct; P19456; 3.
DR   STRING; P19456; -.
DR   PRIDE; P19456; -.
DR   ProMEX; P19456; -.
DR   EnsemblPlants; AT4G30190.1; AT4G30190.1; AT4G30190.
DR   GeneID; 829142; -.
DR   GenomeReviews; CT486007_GR; AT4G30190.
DR   KEGG; ath:AT4G30190; -.
DR   NMPDR; fig|3702.1.peg.20995; -.
DR   TAIR; At4g30190; -.
DR   eggNOG; KOG0205; -.
DR   GeneTree; EPGT00050000005325; -.
DR   InParanoid; P19456; -.
DR   OMA; HRAIAVE; -.
DR   PhylomeDB; P19456; -.
DR   ProtClustDB; CLSN2683068; -.
DR   ArrayExpress; P19456; -.
DR   Genevestigator; P19456; -.
DR   GermOnline; AT4G30190; Arabidopsis thaliana.
DR   GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IDA:UniProtKB.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006534; ATPase_P-typ_PM_proton-efflux.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 3.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; ARATH_4.PE3920; -.
KW   AT4G30190pg.C_scaffold_1320000031; AT4G30190.1.C_scaffold_1320000031;
KW   C0Z2R2; AK318876; AL109796; AL161576; AY035075; BT000781; BT001969;
KW   J05570;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell membrane; Complete proteome; Hydrogen ion transport; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   948 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSLEDIKNE TVDLEKIPIE EVFQQLKCSR EGLTTQEGED RIQIFGPNKL EEKKESKLLK
     FLGFMWNPLS WVMEMAAIMA IALANGDGRP PDWQDFVGII CLLVINSTIS FIEENNAGNA
     AAALMAGLAP KTKVLRDGKW SEQEAAILVP GDIVSIKLGD IIPADARLLE GDPLKVDQSA
     LTGESLPVTK HPGQEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL
     TAIGNFCICS IAIGMVIEII VMYPIQRRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG
     SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC KGVEKDQVLL
     FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDGSGNWHR
     VSKGAPEQIL ELAKASNDLS KKVLSIIDKY AERGLRSLAV ARQVVPEKTK ESPGAPWEFV
     GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGT
     HKDANLASIP VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD
     IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF
     MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT PDSWKLKEIF ATGVVLGGYQ
     AIMTVIFFWA AHKTDFFSDT FGVRSIRDNN HELMGAVYLQ VSIISQALIF VTRSRSWSFV
     ERPGALLMIA FLIAQLIATL IAVYANWEFA KIRGIGWGWA GVIWLYSIVT YFPLDVFKFA
     IRYILSGKAW LNLFENKTAF TMKKDYGKEE REAQWALAQR TLHGLQPKEA VNIFPEKGSY
     RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVVKLKGLDI ETPSHYTV
//

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