ATC_PLAFK
ID ATC_PLAFK Reviewed; 1228 AA.
AC Q08853;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Calcium-transporting ATPase;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump;
GN Name=ATP6;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8314897; DOI=10.1242/jcs.104.4.1129;
RA Kimura M., Yamaguchi Y., Takada S., Tanabe K.;
RT "Cloning of a Ca(2+)-ATPase gene of Plasmodium falciparum and comparison
RT with vertebrate Ca(2+)-ATPases.";
RL J. Cell Sci. 104:1129-1136(1993).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of the calcium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; X71765; CAA50664.1; -; Genomic_DNA.
DR PIR; S37621; S37621.
DR AlphaFoldDB; Q08853; -.
DR SMR; Q08853; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 3.A.3.2.31; the p-type atpase (p-atpase) superfamily.
DR BRENDA; 7.2.2.10; 4889.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1110.10; -; 3.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Calcium transport; Ion transport; Magnesium;
KW Membrane; Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1228
FT /note="Calcium-transporting ATPase"
FT /id="PRO_0000046227"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..994
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 995..1000
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1043..1067
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1068..1118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1119..1140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1141..1151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1152..1172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1173..1185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1186..1206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1207..1228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 452..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="4-aspartylphosphate intermediate"
FT BINDING 716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1228 AA; 139415 MW; 9A6EA4ABF4684079 CRC64;
MEEVIKNAHT YDVEDVLKFL DVNKDNGLKN EELDDRRLKY GLNELEVEKK KSIFELILNQ
FDDLLVKILL LAAFISFVLT LLDMKHKKIE ICDFIEPLVI VLILILNAAV GVWQECNAEK
SLEALKELQP TKAKVLRDGK WEIIDSKYLY VGDIIELSVG NKTPADARII KIYSTSLKVE
QSMLTGESCS VDKYAEKMED SYKNCEIQLK KNILFSSTAI VCGRCIAVVI NIGMKTEIGH
IQHAVIESNS EDTQTPLQIK IDLFGQQLSK IIFVICVTVW IINFKHFSDP IHGSFLYGCL
YYFKISVALA VAAIPEGLPA VITTCLALGT RRMVKKNAIV RKLQSVETLG CTTVICSDKT
GTLTTNQMTT TVFHLFRESD SLTEYQLCQK GDTYYFYESS NLTNDIYAGE SSFFNKLKDE
GNVEALTDDG EEGSIDEADP YSDYFSSDSK KMKNDLNNNN NNNNNSSRSG AKRNIPLKEM
KSNENTIISR GSKILEDKIN KYCYSEYDYN FYMCLVNCNE ANIFCNDNSQ IVKKFGDSTE
LALLHFVHNF DILPTFSKNN KMPAEYEKNT TPVQSSNKKD KSPRGINKFF SSKNDNSHIT
STLNENDKNL KNANHSNYTT AQATTNGYEA IGENTFEHGT SFENCFHSKL GNKINTTSTH
NNNNNNNNNS NSVPSECISS WRNECKQIKI IEFTRERKLM SVIVENKKKE IILYCKGAPE
NIIKNCKYYL TKNDIRPLNE TLKNEIHNKI QNMGKRALRT LSFAYKKLSS KDLNIKNTDD
YYKLEQDLIY LGGLGIIDPP RKYVGRAIRL CHMAGIRVFM ITGDNINTAR AIAKEINILN
KNEGDDEKDN YTNNKNTQIC CYNGREFEDF SLEKQKHILK NTPRIVFCRT EPKHKKQIVK
VLKDLGETVA MTGDGVNDAP ALKSADIGIA MGINGTEVAK EASDIVLADD NFNTIVEAIK
EGRCIYNNMK AFIRYLISSN IGEVASIFIT ALLGIPDSLA PVQLLWVNLV TDGLPATALG
FNPPEHDVMK CKPRHKNDNL INGLTLLRYI IIGTYVGIAT VSIFVYWFLF YPDSDMHTLI
NFYQLSHYNQ CKAWNNFRVN KVYDMSEDHC SYFSAGKIKA STLSLSVLVL IEMFNALNAL
SEYNSLFEIP PWRNMYLVLA TIGSLLLHVL ILYIPPLARI FGVVPLSAYD WFLVFLWSFP
VIILDEIIKF YAKRKLKEEQ RTKKIKID
