ATC9_SCHPO
ID ATC9_SCHPO Reviewed; 1315 AA.
AC O74431;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable cation-transporting ATPase C1672.11c;
DE EC=7.2.2.-;
GN ORFNames=SPCC1672.11c;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20449.1; -; Genomic_DNA.
DR PIR; T41055; T41055.
DR RefSeq; NP_587882.1; NM_001022874.2.
DR AlphaFoldDB; O74431; -.
DR SMR; O74431; -.
DR BioGRID; 275332; 3.
DR STRING; 4896.SPCC1672.11c.1; -.
DR iPTMnet; O74431; -.
DR MaxQB; O74431; -.
DR PaxDb; O74431; -.
DR PRIDE; O74431; -.
DR EnsemblFungi; SPCC1672.11c.1; SPCC1672.11c.1:pep; SPCC1672.11c.
DR GeneID; 2538749; -.
DR KEGG; spo:SPCC1672.11c; -.
DR PomBase; SPCC1672.11c; -.
DR VEuPathDB; FungiDB:SPCC1672.11c; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_3_1_1; -.
DR InParanoid; O74431; -.
DR OMA; GFKFYED; -.
DR PhylomeDB; O74431; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O74431; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0098655; P:cation transmembrane transport; ISM:PomBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF12409; P5-ATPase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1315
FT /note="Probable cation-transporting ATPase C1672.11c"
FT /id="PRO_0000046352"
FT TOPO_DOM 1..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..1072
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1073..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1092..1099
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1100..1117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1118..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1136..1159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1160..1180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1181..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1204..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1217..1236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1237..1253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1254..1274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1275..1315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 619
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1015
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1019
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1315 AA; 148787 MW; 081A550E59F2B0B5 CRC64;
MASPKMIRSK RSTSSIASKN SLNSYLASSL MSHDSIFDGP GLGTSIPSSV SSFHHQTLRP
SSDASVSQFS MDYLQSEYNL NRYNDGESIA ASRDYQSLLR DNGSGVYSDE EEITEMMLEE
LNIHPVLRRE SVGEAAGLSE DGCCQILYLV EEDLEVGIAG YKTNKSRYRL YQAICLLTLG
LAYLIFRWLP KYFIRFVGTR EPLATADWLT IETQWGELSK LDIQIQPYEN SLSSIFGASI
RVAAPEGTEN DPFIENFRYV NYRYMKLIFH PLLDRFLIQQ DWKDPRWIRD TSVVKEGLER
DAINDRLCIF GENLIDLELK SVSQLLIDEV LHPFYIFQVF SIILWSMDSY YYYAICILII
SVVSILGSLI ETRKTLRRMR EMSRFTCPVR VYRDGFWTSI SSTDLVIGDV FEISDPELTI
FPADALLLSG DCIVNESMLT GESIPVSKIP ATDQSMKELF SFSKNIPASL CKHFLFSGTK
IIQVRKPFVN EKEEGASLAM VVRTGFNTTK GALVRSMIFP KPTNFSFYRD SFRFITAMFI
IALIGFVFSS INLLTLGVPI ATIIIRALDL ITIVVPPALP ATLTIGTTFA ISRLRKQGIF
CISPQRVNVS GKLDLISFDK TGTLTEDGLD IMGVSVIEGS ELGDLRSNSG NLCSKDLLSN
DSPSNLLYTM ATCHMLRYVD GELVGDPLDI KMFKFTHWSY SEENFLNKKM SSEQAEDAAY
VRTQQLIPPT VSPPWNSPSN NYTESDLELG IVRTFEFVSQ LRRMAVIVKH GKFKKMDAYV
KGAPEIMPSI CKPESFPANY QEVLDYYTHN GFRVIACASK QLENCTWAKA QRMKREQVEC
DLDFCGFIVF ENKLKSTTAT VIRELNDARI RTVMCTGDNV LTSICVGKRC GMLPEDGYVF
LPRFDEESES ADEASRQLVW QAIENNEIFL DPHTLRPNVD FADHEPVSIE LARLKDFHIA
LTGDVFRWLV DYAPLNVFHH ILLKAQIFAR MSPSEKNELV SCFQNLNYCV GFCGDGANDC
GALKAADVGI SLSEAEASVA APFTSKWFEI TCVLDVIKDG RAALVTSFSC FQYMALYSAI
QFITVSILYT TNSNLGDFQF LFIDLVIILP IAVFMGRSRP YHRLAHKRPT ANLVSKRILS
PLIGQIVLIC IIQYITLRIV RREPWYIPPP ANSSDTNITN SDVTALFLIS CFQYIFIGVV
LSIGPPYREK VWRNYSFTAV VVVLLILTVK LIRLQNHKNF FMKLFQLTPT SKSFQNFLIF
AGVIYYLLAA SGQNYIFISM TNFISHLNNR LLNRRTKVSK KLYKRLFADL QNEQV
