ID I0YY62_COCSC Unreviewed; 1063 AA.
AC I0YY62;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=COCSUDRAFT_23431 {ECO:0000313|EMBL:EIE23331.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE23331.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE23331.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE23331.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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}.
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:EIE23331.1}.
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DR EMBL; AGSI01000007; EIE23331.1; -; Genomic_DNA.
DR RefSeq; XP_005647875.1; XM_005647818.1.
DR AlphaFoldDB; I0YY62; -.
DR STRING; 574566.I0YY62; -.
DR GeneID; 17041319; -.
DR KEGG; csl:COCSUDRAFT_23431; -.
DR eggNOG; KOG0205; Eukaryota.
DR OrthoDB; 46741at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
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; 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:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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 Reference proteome {ECO:0000313|Proteomes:UP000007264};
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 83..108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 114..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 307..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 705..726
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 875..899
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 943..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 38..110
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 1063 AA; 115246 MW; 03F7DB413617685D CRC64;
MAENGTNGVN GVKAENGKGD VEAPPTAAAA VDTGKAVDFA KISIAEAFKT LKASEEGLDG
AEVKRRLDQY GYNKLPESTR IPFLVFLGYL WNPLSWAMEV AAILAIILLD YADFALIVAL
LLVNATISFV EESNADKAIK ALTAALAPKA RVKRDGKVST VEAKELVPGD IIIVMFGNIV
PADIKLLGKE NDPTEAPMQI DQAALTGESL PAKKYSGNVA FSGSTVKQGE KEALVYATGE
NTFFGRAAAL ISGTHNVANL QKIMTRIGGT CLVTIGIWCI IELAVQFGHY KHVCRMGEEG
CPTLTNMLVI IVGGIPIAMP TVLSVTLALG AYKLAKEGAI VARMSAVEEM AGMDILCSDK
TGTLTLNQLS VDKPTCMVVG PEGRTLDEVL KWGALSANIV SEEPIDVVLH EAYDGHDTLW
NDYKLQKFVP FNPTDKYTIA TVKNNKTGES TRIMKGAPQV VLKKSYNYSE IGDSVHNKIT
EFAGRGFRAL GVATAPDDGT EVEKARWDFQ VLLPLFDPPR HDTKETIERC IEKGISVKMV
TGDQLLIGKE TAKQLGMGTN MYTTEVLLNA KEGKGQLPPE LAHVKDVDEL VEHADGFAEV
FPEHKFEIVN ILKGRKHIVG MTGDGVNDAP ALKKADVGIA VDGATDAARG AADIVLTRPG
LSVIVSAIIG ARKIFQRMTT YSKYTVAMTF RICFTFGLLT VIYDWYFPTI LIVMLAVFND
GAMIALSKDR VISSPVPNTW NLKNIFTVGI VYGLYLTLSS WVLFYVVTHM TFFADKCNLA
DLNNTDEVLR PYCERMITGM GLAPGAPVTS VYPGQDGKDA NLEGVTALDQ CITEQIYVRD
GITRSLLYNQ VSISGQALVF VVRTSGWSII SRAGLYTYIA FFAAQVGSTL IAAIGFAAYT
HPRDAWAFDG PAKFTQLSNG HGPAFFGNSV VPIHGTEGEF TPSVIGCTYY VIVAWIWSLI
WYIGLDPIKW ALMYILNEDG WRNKSAFKAE QKAAVRTQVE EPVGVAGFER VSYSNPLGRR
SVTAAAQRPN FLERASVVMV DDSGLTRAPD GKLDHKSLTP KDP
//
