ATC1_DICDI
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 03-AUG-2022, entry version 152.
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 (Slime mold).
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.DDB0214945; -.
DR TCDB; 3.A.3.2.17; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P54678; -.
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; IMFWGDK; -.
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:0016021; C:integral component of membrane; TAS:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
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; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
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
