ID   Q9FNS3_CHLRE            Unreviewed;      1053 AA.
AC   Q9FNS3;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   Name=pmh1 {ECO:0000313|EMBL:CAC19368.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:CAC19368.1};
RN   [1] {ECO:0000313|EMBL:CAC19368.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Campbell A.M., Coble A.J., Cohen L.D., Ch'ng T.H., Russo K.M., Long E.M.,
RA   Armbrust E.V.;
RT   "Identification and DNA sequence of a new H+-ATPase in the unicellular
RT   green alga Chlamydomonas reinhardtii (Chlorophyceae).";
RL   J. Phycol. 37:536-542(2001).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362083}.
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DR   EMBL; AJ300672; CAC19368.1; -; Genomic_DNA.
DR   ExpressionAtlas; Q9FNS3; baseline.
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   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; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF48; 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; 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; 2.
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        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        607..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        703..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        734..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        781..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        822..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        860..880
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          8..72
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  114933 MW;  ABC93193F4247C79 CRC64;
     MAEQEKPKEE HAPINFDENH EEKQAEELIK VHGRNELEEK HTPSWLIFLR QLYQPMPIMI
     WIAAIVEGAI ENWADMGILL GIQFINATLR LVGQAYETTK AGDAVAALKA SLKPLATAKR
     DGKWANIDAG NLVPGDLVLL ASGSAVPADC LINHGTVDID QAALTGESLP VTMHKGDSAK
     MGSTVVRGET EATVEFTGKN TFFGKTASML QQSGGELGHL QKILLTIMFV LVVTSFILFT
     VVLLVASIPI AIEIVCTTTL ALGSRELSRH GAIVTRLAAI EDMAGMNMLC SDKTGTLTLN
     KMAIQDDTPT YLPGLDQRKL LHLGALAAKW HEPPRDALDT LVLTCETQDL SALDVYEQID
     YMPFDPTVKR TEGTIKDKRD GTTFKVTKGA PHIILKLTHD ERIHHMVDET VAAFGQRGIR
     CLAIARTLGD DLNTWHMAGL LTFLDPPRPD TKDTIHKVMA YGVDVKMITG DNILIAKETA
     RVLGMGTNIQ DPKSLPTMDA EGKAPKDLGK KYGKIIMEAD GFAQVYPEHK YLIVEALRQN
     GFACGMTGDG VNDAPALKRA DVGVAVQGAT APLAPPPTIV LTEPGLSTIV HGIVTARCIF
     QRMKNFINYR IAATLQLLTF FFIAVFALPP IDYPQGMWPT CNTPAAVGSP TCCPETYTYD
     NVTSTVTMEW LRDNQGNDEI ANNLNGVCFT DGEPWPDFFK MPVLMLMLIT LLNDGTLISI
     GYDHVKPSAM PEKWNLPALF AISIVLGMVA CGSSLLLLWA ALDSWNTNGI FQKWGLGGMP
     YGKVTTIIYL KVSVSDFLTL FSARTHDGFF WSARPSPILM GAALLALSLS TILACVWPKG
     HTDKQLSMGL AYETDPHSNT LMPLWIWIYC VFWWFVQDFM KVAAYWMMHR YNWFDINTSM
     AINKRDANKV DDRHDPLARG SVGLVEGKLL AAKVEEAQAK VNAAIKHDQA TNLGRASANX
     GRVSANLKQA GMARHSGNPK GADVEGAAQT VENVLLHLDE ARGELDPKVQ QEIAPAIEGV
     REAAEKLAAN TAAALGGANP EQTLAKISSK RHM
//