UniProt: Q9M4N4

Database: UniProt
Entry: Q9M4N4_MEDTR

LinkDB:  Q9M4N4_MEDTR 
Original site:  Q9M4N4_MEDTR

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (22)   

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ID   Q9M4N4_MEDTR            Unreviewed;       965 AA.
AC   Q9M4N4;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   Name=ha1 {ECO:0000313|EMBL:CAB85494.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:CAB85494.1};
RN   [1] {ECO:0000313|EMBL:CAB85494.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Philipp F.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAB85494.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krajinski F., Gianinazzi-Pearson V., Franken P.;
RT   "Mtha1, an arbuscular mycorrhiza-regulated H+-ATPase gene from Medicago
RT   truncatula.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001250,
CC         ECO:0000256|RuleBase:RU362083};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC       ECO:0000256|RuleBase:RU362083}.
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DR   EMBL; AJ132891; CAB85494.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9M4N4; -.
DR   ExpressionAtlas; Q9M4N4; differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 6.10.140.890; -; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861:SF54; ATPASE 7, PLASMA MEMBRANE-TYPE; 1.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
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   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW   Hydrolase {ECO:0000313|EMBL:CAB85494.1};
KW   Ion transport {ECO:0000256|RuleBase:RU362083};
KW   Magnesium {ECO:0000256|RuleBase:RU362083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362083};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362083};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        106..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        253..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        287..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        654..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        719..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        801..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        832..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          17..89
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   965 AA;  105620 MW;  0C753756162BDEE8 CRC64;
     MVEGTMSLDA VIKEAVDLEN IPIDEVFDNL KCTKEGLTCE EVQERLELFG YNKLEEKKES
     KILKFLGFMW NPLSWVMEAA AIMAIAMAHG GRNMDGTKKQ GDYQDFVGII ILLIINSTIS
     FIEENNAGNA AAALMARLAP KAKVLRDGKW SEEDASVLVP GDIVSIKLGD IIPADARLLE
     GDPLKIDQSA LTGESLPVTK HPGEGIYSGS TCKQGEIEAI VIATGVHTFF GKAAHLVENT
     THVGHFQKVL TSIGNFCICS IAIGMVIEII VIYGVHGKGY RNGIDNLLVL LIGGIPIAMP
     TVLSVTMAIG SHKLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLT VDKDMIEVFA
     KGVDKDLVVL MAARASRLEN QDAIDCAIVS MLADPKEART GIKEVHFLPF NPTDKRTALT
     YIDAAGNMHR VSKGAPEQIL NLARNKAEIA QKVHSMIDKF AERGLRSLGV ARQEVPEGSK
     DSPGGPWEFV ALLPLFDPPR HDSAETIRRA LDLGVSVKMI TGDQLAIGKE TGRRLGMGTN
     MYPSSSLLGD NKDQLGAVSI DDLIENADGF AGVFPEHKYE IVKRLQARKH ICGMTGDGVN
     DAPALKIADI GIAVADSTDA ARSASDIVLT EPGLSVIISA VLTSRAIFQR MKNYTIYAVS
     ITIRIVLGFM LLNSFWSFDS PPFMVLIIAI LNDGTIMTIS KDRVKPSPLP DSWKLSEIFA
     TGVILGTYLA IMTVIFFWIV METNFFPNFG VHRFRPDLKA PVTSEMTEKL ASAVYLQVST
     ISQALIFVTR SRGWSYTERP GLLLVFAFAI AQLVATVISA QATWKIAGIR GIGWGWAGVI
     WLFNIVTYVF LDPLKFVVAY QQSGRAWNLV VNQRTAFTNK NDFGKEAREA AWAAEQRTLH
     GLRSAEIKGF AEKHNHREIN TMADEAKRRA ELARLRELHT LKGRVESFAK LRGLDIDTMN
     GHYTV
//

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