ATC2_SCHPO
ID ATC2_SCHPO Reviewed; 1292 AA.
AC Q9HDW7; Q9UTX0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calcium-transporting ATPase 2;
DE EC=7.2.2.10;
GN Name=pmc1; ORFNames=SPAPB2B4.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 161-331.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP IDENTIFICATION.
RX PubMed=12707717; DOI=10.1007/s00294-003-0395-2;
RA Okorokova-Facanha A.L., Okorokov L.A., Ekwall K.;
RT "An inventory of the P-type ATPases in the fission yeast
RT Schizosaccharomyces pombe.";
RL Curr. Genet. 43:273-280(2003).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15470240; DOI=10.1128/ec.3.5.1124-1135.2004;
RA Cortes J.C.G., Katoh-Fukui R., Moto K., Ribas J.C., Ishiguro J.;
RT "Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and
RT is required for polarized cell growth and cytokinesis.";
RL Eukaryot. Cell 3:1124-1135(2004).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. Transports the calcium to
CC the vacuole and participates in the control of the cytosolic free
CC calcium. {ECO:0000269|PubMed:15470240}.
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: Vacuole membrane {ECO:0000269|PubMed:15470240};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15470240}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAC21470.1; -; Genomic_DNA.
DR EMBL; AB027950; BAA87254.1; -; Genomic_DNA.
DR RefSeq; NP_593890.1; NM_001019320.2.
DR AlphaFoldDB; Q9HDW7; -.
DR SMR; Q9HDW7; -.
DR BioGRID; 279897; 18.
DR STRING; 4896.SPAPB2B4.04c.1; -.
DR TCDB; 3.A.3.2.35; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9HDW7; -.
DR MaxQB; Q9HDW7; -.
DR PaxDb; Q9HDW7; -.
DR PRIDE; Q9HDW7; -.
DR EnsemblFungi; SPAPB2B4.04c.1; SPAPB2B4.04c.1:pep; SPAPB2B4.04c.
DR GeneID; 2543477; -.
DR KEGG; spo:SPAPB2B4.04c; -.
DR PomBase; SPAPB2B4.04c; pmc1.
DR VEuPathDB; FungiDB:SPAPB2B4.04c; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; Q9HDW7; -.
DR OMA; KTAHVGF; -.
DR PhylomeDB; Q9HDW7; -.
DR Reactome; R-SPO-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-SPO-5578775; Ion homeostasis.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q9HDW7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IDA:PomBase.
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:0005524; F:ATP binding; IC:PomBase.
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; ISM:PomBase.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISO:PomBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:PomBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:PomBase.
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 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Calcium transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..1292
FT /note="Calcium-transporting ATPase 2"
FT /id="PRO_0000362141"
FT TOPO_DOM 1..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..273
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..488
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 960..966
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 988..1016
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1084
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1106..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1137..1292
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 545
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 691
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 807..809
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 862
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 881
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 947
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 977
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 981
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 981
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
SQ SEQUENCE 1292 AA; 142235 MW; 1499E90144A2B07B CRC64;
MPTYNDDDDS SRPPSVHSER NQKPSSSQFL GVPSSNYNQR ENSSRSGSST ISREPSSSGT
MYPMASRDSM KESYDKNKGT PPDYTSYVSH SDAEPEQASS KSSTSIEDLL HTEYDDAPFA
FSIPLLQRLQ DPKNTSLLHA IHGLKGLCKG LKVDPSTGIS THEPHYADKL QMSDILNDDS
NPKLVVHLDR IRSQDNNPEA KVSHDSDRVK YYGKNVLPEH DSKGLIRLML EAFKDKVLIL
LSIAAVVSLA LGLYQTFGQP PTLDPITGKP EPRVEWVEGV AIMAAIVIVV TVGGVNDWQK
ELQFKKLNAK VSNFDVQVLR DGAVHSTSVF DLVVGDVLFV EAGDVVPVDG VLIESNNLVL
DESAMTGETD NIKKVDANTA IERTSPDVEY RKNADPYLIS GTTILEGNGK LLVTAVGVNS
FNGRTTMAMR TEGQATPLQL RLSRVADAIA KLGGAASALL FIVLLIEFLV RLKSNDSSSK
NKGQEFLQIL IVSVTLLVVA VPEGLPLAVT LALAFATNRM QKDNNLVRHL QACETMGTAT
NICSDKTGTL TQNRMTVVAG GFGTDVLFFD HNDETPTNVD QGSDSSKFED AGASAFAFKR
LSPELRDLTL YSIAVNSTCR QLFEDNSDTP RFIGSKTETA LLDMSVKELG LTNVDSMRSS
VDIKQFFSFS SDRKASGAIF EYKDKYYFVV KGMPERVLQQ STSVITNGSL DEVEDMHSHA
DYFKEMITGY AKRSLRTLGL CYRVFDSWPP KDIPTNDEDS SNPLKWEDAF TDMTFLGFFG
IMDPIRPDVP LAVKVCQGAG VTVRMVTGDN IVTAKAIASQ CGIYTEDGIS MEGPEFRSLS
DEKRLEILPK LDVLARSSPL DKQLLIEGLQ KLGNVVAVTG DGTNDAPALK KANVGFSMGK
SGTEVAKEAS DIILMDDNFS SIVKAIAWGR TVNDAVKKFL QFQITVNITA VFLTIISAVA
STDQSSVLTA VQLLWVNLIM DTLAALALAT DPPTPEVLKR KPEKPGASLF TFDMWKMIIC
QSMYQLAVTL VLHFAGNSIF HYPSNTADMN TIVFNTFVWL QLFNEINNRR LDNKLNIFER
INHNFLFIAI FVIVAGIQVI IVFFGGAAFS VKRIDGKGWA ISIVFGVISI PLGALIRCVP
NNFLRKVLPV KTIDTVFSWI LNPRFRSKRR STDHDVESLS LIPYEPTSPN EVIDSIRHSL
GFVQRIRGGR IRHLLNNSKF DKQMEALPER LRPRVKQRFM KIRSPSVSSA TSVALMIPIS
TLVSEASGRL GGHDIWISHN RQALDKKSSN VH
