ID   ATC1_DICDI              Reviewed;        1115 AA.
AC   P54678; Q54YN8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Calcium-transporting ATPase PAT1;
DE            Short=PAT1 {ECO:0000303|PubMed:7499325, ECO:0000303|PubMed:9885293};
DE            EC=7.2.2.10 {ECO:0000269|PubMed:9885293};
GN   Name=patA; ORFNames=DDB_G0277861;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   STRAIN=AX3;
RX   PubMed=7499325; DOI=10.1074/jbc.270.47.28276;
RA   Moniakis J., Coukell M.B., Forer A.;
RT   "Molecular cloning of an intracellular P-type ATPase from Dictyostelium
RT   that is up-regulated in calcium-adapted cells.";
RL   J. Biol. Chem. 270:28276-28281(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9885293; DOI=10.1242/jcs.112.3.405;
RA   Moniakis J., Coukell M.B., Janiec A.;
RT   "Involvement of the Ca2+-ATPase PAT1 and the contractile vacuole in calcium
RT   regulation in Dictyostelium discoideum.";
RL   J. Cell Sci. 112:405-414(1999).
CC   -!- FUNCTION: Calcium ATPase involved in Ca(2+) homeostasis as a component
CC       of the contractile vacuole complex. {ECO:0000269|PubMed:7499325,
CC       ECO:0000269|PubMed:9885293}.
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         Evidence={ECO:0000269|PubMed:9885293};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000269|PubMed:9885293};
CC   -!- SUBCELLULAR LOCATION: Contractile vacuole membrane
CC       {ECO:0000269|PubMed:9885293}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9885293}. Cell membrane
CC       {ECO:0000269|PubMed:7499325}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:7499325}. Note=Contractile vacuole complex.
CC       Localizes to the contractile vacuole membrane in unstimulated cells
CC       (PubMed:9885293). Localizes to the cell membrane and the contractile
CC       vacuole membrane in cells stimulated by calcium (PubMed:9885293).
CC       {ECO:0000269|PubMed:9885293}.
CC   -!- DEVELOPMENTAL STAGE: Expressed constitutively at very low levels during
CC       vegetative growth and throughout development.
CC       {ECO:0000269|PubMed:7499325}.
CC   -!- INDUCTION: By calcium. {ECO:0000269|PubMed:7499325,
CC       ECO:0000269|PubMed:9885293}.
CC   -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) displays
CC       impaired growth in high Ca(2+) medium but normal growth in low Ca(2+)
CC       medium. Antisense inhibition does not affect development in high Ca(2+)
CC       medium.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
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DR   EMBL; X89369; CAA61551.1; -; mRNA.
DR   EMBL; AAFI02000023; EAL68103.2; -; Genomic_DNA.
DR   PIR; S57726; S57726.
DR   RefSeq; XP_642164.2; XM_637072.2.
DR   AlphaFoldDB; P54678; -.
DR   SMR; P54678; -.
DR   STRING; 44689.P54678; -.
DR   TCDB; 3.A.3.2.17; the p-type atpase (p-atpase) superfamily.
DR   PaxDb; 44689-DDB0214945; -.
DR   EnsemblProtists; EAL68103; EAL68103; DDB_G0277861.
DR   GeneID; 8621371; -.
DR   KEGG; ddi:DDB_G0277861; -.
DR   dictyBase; DDB_G0277861; patA.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; P54678; -.
DR   OMA; MWIAFND; -.
DR   PhylomeDB; P54678; -.
DR   Reactome; R-DDI-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-DDI-5578775; Ion homeostasis.
DR   Reactome; R-DDI-936837; Ion transport by P-type ATPases.
DR   PRO; PR:P54678; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031164; C:contractile vacuolar membrane; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:dictyBase.
DR   GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; TAS:dictyBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; TAS:dictyBase.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; IDA:dictyBase.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IDA:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 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; 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   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Vacuole.
FT   CHAIN           1..1115
FT                   /note="Calcium-transporting ATPase PAT1"
FT                   /id="PRO_0000046179"
FT   TOPO_DOM        1..99
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..126
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..235
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..287
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..328
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..735
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        736..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        757..832
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        833..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        854..873
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        874..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        895..913
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        914..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        935..943
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        944..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        965..1115
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   REGION          762..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        385
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         678
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         682
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        212
FT                   /note="C -> Y (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="L -> H (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289..290
FT                   /note="GY -> WL (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="G -> V (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        643
FT                   /note="A -> V (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        680
FT                   /note="T -> S (in Ref. 1; CAA61551)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1115 AA;  120677 MW;  6A80A21D490973AB CRC64;
     MTGSHEMESI MLDSMEEEFP VSVETLGKLV DVPKGFDTYA ELGGLSGLST KLKSNIKTGL
     PLEKSSTEEN RVLKYSKNIL PDPPHQPLWS IVLDALSDHI LILLIVAAVV SIVLGSIDYT
     SDHPETGWID GVAILVAVIL VVGITSLNDF KNQARFRELN DKSNDKEVKG IRGGEQCQIS
     IFDVKVGDII SLDTGDIICA DGVFIEGHAL KCDESSITGE SDPIKKGQPQ DNMDPFLISG
     SMVIEGFGTM LVTAVGVNSF NGKTMMGLRV ASEDTPLQMK LSVLASRIGY FGMGAAILML
     LIAIPKYFIQ RKVHDIEITR EDAQPIVQLV ISAITIVVVA VPEGLPLAVT MALAYGMMKM
     FKENNLVRNL ASCETMGSAT TICSDKTGTL TQNVMSVVTG TICGVFPTLD GIAQKIPKHV
     QSILTDGMAI NSNAYEGVSS KGKLEFIGSK TECALLNFGK LFGCDYNEVR KRLEVVELYP
     FSSARKRMSV LVKHDQNLRL FTKGASEIIL GQCGSYLDEA GNIRPISEAK AYFEEQINNF
     ASDALRTIGL AYRDFQYGEC DFKEPPENNL VFIGIVGIKD PLRPEVPEAV EICKRAGIVV
     RMVTGDNLVT AQNIARNCGI LTEGGLCMEG PKFRELSQSE MDAILPKLQV LARSSPTDKQ
     LLVGRLKDLG EVVAVTGDGT NDGPALKLAN VGFSMGISGT EVAIAASDVV LLDDNFASIV
     RAVLWGRNIY DAICKFLQFQ LTVNVVAVTV AFIGTLTSDV VEDKDNSSSS GSADKVTEEE
     PRQGSPLTAV QLLWVNLIMD TLAALALATE PPTPELLERP PNGKNAPLIT RSMWKNIIGQ
     AALQLAILFT ILYQGHNIFQ HFVPQAHGPI IKNGLHHYTL VFNCFVFLQL FNEINARVLG
     SRTNPFKNFF NNPIFIAVMI FTLGVQIIFV TFGGSATSTD SLYIVEWICC VVVGAISLPV
     GLLLRKIPIR EPVVKNEIPV HSEAVYTSPS PNPSSSNLLG SGGAKPISKD YPTSGESTPP
     INDEGSPLVT RKTSVGASAN DNINTPIPSS SSNLVNLNKP TQVGRGWQIV RQTHKKLVVI
     NALKEFSQNK EPGLVDVVRG TNRGSLHLPV NQINN
//