ID A0AAD5E275_UMBRA Unreviewed; 750 AA. AC A0AAD5E275; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 24-JUL-2024, entry version 2. DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083}; DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083}; GN ORFNames=K450DRAFT_258733 {ECO:0000313|EMBL:KAI8576066.1}; OS Umbelopsis ramanniana AG. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Umbelopsidomycetes; Umbelopsidales; Umbelopsidaceae; Umbelopsis. OX NCBI_TaxID=1314678 {ECO:0000313|EMBL:KAI8576066.1, ECO:0000313|Proteomes:UP001206595}; RN [1] {ECO:0000313|EMBL:KAI8576066.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AG {ECO:0000313|EMBL:KAI8576066.1}; RG DOE Joint Genome Institute; RA Mondo S.J., Amses K.R., Simmons D.R., Longcore J.E., Seto K., Alves G.H., RA Bonds A.E., Quandt C.A., Davis W.J., Chang Y., Letcher P.M., Powell M.J., RA Kuo A., Labutti K., Pangilinan J., Andreopoulos W., Tritt A., Riley R., RA Hundley H., Johnson J., Lipzen A., Barry K., Berbee M.L., Buchler N.E., RA Grigoriev I.V., Spatafora J.W., Stajich J.E., James T.Y.; RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAI8576066.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AG {ECO:0000313|EMBL:KAI8576066.1}; RX PubMed=36037379; RA Amses K.R., Simmons D.R., Longcore J.E., Mondo S.J., Seto K., RA Jeronimo G.H., Bonds A.E., Quandt C.A., Davis W.J., Chang Y., RA Federici B.A., Kuo A., LaButti K., Pangilinan J., Andreopoulos W., RA Tritt A., Riley R., Hundley H., Johnson J., Lipzen A., Barry K., Lang B.F., RA Cuomo C.A., Buchler N.E., Grigoriev I.V., Spatafora J.W., Stajich J.E., RA James T.Y.; RT "Diploid-dominant life cycles characterize the early evolution of Fungi."; RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022). CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen CC ion pump. The proton gradient it generates drives the active transport CC of nutrients by H(+)-symport. The resulting external acidification CC and/or internal alkinization may mediate growth responses. CC {ECO:0000256|ARBA:ARBA00003417}. 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|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}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU362083}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAI8576066.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MU620963; KAI8576066.1; -; Genomic_DNA. DR Proteomes; UP001206595; Unassembled WGS sequence. DR CDD; cd02076; P-type_ATPase_H; 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; CALCIUM-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR42861:SF21; PLASMA MEMBRANE 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; SFLDS00003; Haloacid_Dehalogenase; 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 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 89..115 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362083" FT TRANSMEM 127..143 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362083" FT TRANSMEM 276..299 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362083" FT TRANSMEM 311..332 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362083" FT TRANSMEM 678..701 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362083" FT DOMAIN 44..116 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 750 AA; 81531 MW; 69E72203101439CA CRC64; MASTDPNAEK QEPKVEQQDA ATNVNVPNGM SLTVEELYDK DKFDLSTMEP GDVFQLLQTT TEGLTSTEAA ARIEKFGYNR LEHKEVNPFL QFLGFMWNPL SWVMEAAAIV AIALSNGGGR APDWPDFVGI ILLLLANSII GFMEERQAGN AVKALMESLA PEAKVKRDGE WKTIEAAELV PGDVISIKLG DVIPADGRLV AAHGQVSIDQ AALTGESLPV TKEAGDEIFS GSTCKQGEAQ AIVIGTGLNT FFGRAAKLVG DANDEMGHLQ VILAKIGNFC MCTIGIFLVL EILVMYPAFK YDYRRGIDNL LVLLIGGIPI AMPTVLSVTL AIGAKQLAEH KAIVTRITAI EEMAAVTILC SDKTGTLTLN KLIVDKPTVK SYADYNIEEI IQFSAYACRT ENQDAIDFCI CNSLPDVKLA RDGIEEMEFK PFNPVIKRTE ITYKDAEGVV RRVTKGMSHT ILDLCTRDKT EEQIKALNDD VDEYARRGLR ALAVAIDEVP TGGVEDEGRG FKLVGLLPIY DPPRSDTKET IDRAIALGVS VKMITGDQLA IAKETGRRLG MGDNMFLSKT LKDGPPAGSG YSDMDELVLQ ADGFAGVYPE HKYEIVERLQ NMGHMTAMTG DGVNDAPALS KANVGIAVAD ASDAARSAAD IVLTEPGLSV IIEAIIGSRQ IFQRMRNYSI YTCSVTIRVV VGFAILCFAF EFDFPPFLVL ILAILNDGTI MTISTDRVST ISQALIFITR SRGFFFTDWV //