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Database: UniProt
Entry: O77368_PLAF7
LinkDB: O77368_PLAF7
Original site: O77368_PLAF7 
ID   O77368_PLAF7            Unreviewed;      1864 AA.
AC   O77368;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   SubName: Full=P-type ATPase, putative {ECO:0000313|EMBL:CAB11124.1};
DE            EC=3.6.3.1 {ECO:0000313|EMBL:CAB11124.1};
GN   ORFNames=PF3D7_0319000 {ECO:0000313|EMBL:CAB11124.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAB11124.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CAB11124.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=10448855; DOI=10.1038/22964;
RA   Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA   Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA   Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA   Jassal B., Kyes S., McLean J., Moule S., Mungall K., Murphy L., Oliver K.,
RA   Quail M.A., Rajandream M.-A., Rutter S., Skelton J., Squares R.,
RA   Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA   Barrell B.G.;
RT   "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT   falciparum.";
RL   Nature 400:532-538(1999).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [3] {ECO:0000313|EMBL:CAB11124.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.,
RA   Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corto C., Cronin A., Davies R.,
RA   Davies P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James D.,
RA   Johnson D., Kerhornou A., Knight A., Kontfortov B., Keyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., McLean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M-A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AL844502; CAB11124.1; -; Genomic_DNA.
DR   PIR; T18485; T18485.
DR   RefSeq; XP_001351260.1; XM_001351224.1.
DR   AlphaFoldDB; O77368; -.
DR   STRING; 36329.O77368; -.
DR   TCDB; 3.A.3.8.28; the p-type atpase (p-atpase) superfamily.
DR   PaxDb; 5833-PFC0840w; -.
DR   EnsemblProtists; CAB11124; CAB11124; PF3D7_0319000.
DR   GeneID; 814504; -.
DR   KEGG; pfa:PF3D7_0319000; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0319000; -.
DR   HOGENOM; CLU_000846_5_2_1; -.
DR   InParanoid; O77368; -.
DR   OMA; TWFVISH; -.
DR   OrthoDB; 227740at2759; -.
DR   PhylomeDB; O77368; -.
DR   Reactome; R-PFA-6798695; Neutrophil degranulation.
DR   Reactome; R-PFA-936837; Ion transport by P-type ATPases.
DR   Proteomes; UP000001450; Chromosome 3.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:P-type ion transporter activity; ISS:GeneDB.
DR   GO; GO:0006812; P:monoatomic cation transport; ISS:GeneDB.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 2.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CAB11124.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        70..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        538..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1496..1521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1533..1550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1638..1659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1679..1700
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1707..1727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1755..1776
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..106
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1466..1601
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   DOMAIN          1626..1782
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          301..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1864 AA;  218020 MW;  6A425F4410B1E667 CRC64;
     MKILEWISCT IKGKHNENKI YLISNFEFNK DDHEYYIKNA ENRIKEEDLN IDIIYGKKHK
     NEIRTAKYKL YSFLPLIVFF QFLRLGNLYF LSISMLQLIP EITDSKGMPT YLIPLVFIIV
     VAMIKEFFED WQRHKSDNEE NSKKTMVFVQ GELKEKKWAD VKDGDVVKIF SYEYFPADLI
     VLNCSNKKGI VNIETKNVDG ESNVKQKYCL PDISKYFSDD KTAGFCRIEL ISERPNDNIF
     DYKGYMILPP LQYKNMKNGK LIHFYNTHYK MDDHKDEHDE KGTGKYINKN YKNDYNDKHI
     SYNTNEQNNL SDMTKNDPKE YDYNPQNEIN NNNNNNNCDN NNNNCNNNNR FFVDDIKKQG
     QNEETVDKKK SFFIINNQKK VYDTGSSNND QITHINNDVI SEKKRASRRR TLYNKLTFNK
     SFFNNKNENK KLNKRNSTLS SINNNNDNNN NNNNNNNNIH NREYDGEEQT LKKENFFFKE
     YKRDQKFVQI TIDNLVLRGT SLVNTKWIYG LVINTGNRTK LMKNASTKSR QKWSRLEFVY
     GNHVIVLIIC QVFISLIVAI AGVLWMRRKG YTLWYLNLDQ TSDSLKTFFI TIGSMVLLFG
     SFIPVDLLLI WEVVRLLQGY LINWDNDMYS EKTGRHALSK AGQLLEEMGN VTHIYSDKTG
     TLTQNVMQLQ NIGLGNKGTY GFYDFSNIKE NITKSRHWGS QDPMDPVLEE YENEENVYSN
     VNDDNKNDHG TNESDDNNNN NNNNDDDDHH DNNHNIHNDQ NNNAQYDNYD NYYLNNHQQQ
     NKVKNRPCID DETNFYRNNN MNKERTRKSY TFLNPLNWSN TSINTKMKKK KSLFYNKNSL
     ANYESLLNNT YTEDDFIRGE NEFVFFNRIL FVNKIYSIRH DVQDQIYFLL LVLSLCHSAM
     IRNVDIDEMD NNEDDNNNNE KLKIYDKETD IVYTYITQTQ PQYDASSPDE LALISTSLYL
     GCEFVNRPNL TTIEIELTST FAQRFILGEK KFEKFLEKKE FYEKEFDTYF PDISACLGKE
     KKKDNNKINE MINNKGNTKD DYMNNFHMSI PIKNIFGSNK MQYKEEIKYE EKIIKKVVPI
     LSFEILDVFA FDNVRKRMSL IVKNEKKEIF MLVKGADTSV LKLASKNQEN IVDHVEHQLH
     AFATSGLRTL VLGYKYLTEN EFSDMYRNHI NARKKSETDK EEYLQEFYEE AENNLIIIGC
     TGIDDKLQDD VPQVIQDLRD AGMTICVLTG DKLETAINIG HSINILNKQT YNAIFTETDP
     TLLLEQLNIH EKNTNAANLL NVDHGTKWWN SVNWEHLNLD LRSETILNFM KSNFHGSLKK
     SIISSNMFNM KNNNSFPSLA RQDKVFNSFL ESSESFCHNN NEMDKTKGKE KVHYSQFSIT
     ITGEALDVIM KDKILKIKFY TLARSASTLI ACRVTPKQKS LLVKENSAFN PRGTSLAIGD
     GANDVGMILM ANVGVGIAGK EGLQAARSSD FTISEFKYLK KLLFVHGRES LRRNSFLVYF
     CIFRNVSFCL CSMILIFWTG YSAIDAWNPW TKQIINIAFT SLPVIFFVAL DKQLPHNILL
     NNPLLYETSP STLWPFYSNR KMEFYTNKVK GCYKSFYKFC FFPIRYIPYI QRYTEKIKSW
     IGKRSKPEKY RTYGTHYLFV YLLFAIWLAT VETVIMLHFS TGQAYSSSLK DNHHVDIDFN
     TFSQILYTHH VIAVNIVVVL MTNTWFFISH VVLWIELIAT FFFWFIISNT KFFLDIIGAD
     ELHGTFEKAH SSGNYYASLI ISLYISILPL IILMTYQFIK KPTMEQIVLE QLKLGKFEGL
     RKHEIKKLAY IDNQKSSNEF THKGFAFAVE AKEAFWGLVQ KAIYKIKMPL VKDETANIKH
     KRKS
//
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