ATC1_SCHPO
ID ATC1_SCHPO Reviewed; 899 AA.
AC O59868;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=Golgi Ca(2+)-ATPase;
GN Name=pmr1; Synonyms=pgak2; ORFNames=SPBC31E1.02c;
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 [GENOMIC DNA], 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kaplan N., Gnoj L., Lodhi M., Johnson A.F., Dedhia N., Parnell L.D.,
RA McCombie W.R.;
RT "S. pombe genomic sequence PGAK, extension of cosmid 800, accession
RT U41410.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=14723709; DOI=10.1111/j.1356-9597.2004.00699.x;
RA Maeda T., Sugiura R., Kita A., Saito M., Deng L., He Y., Yabin L.,
RA Fujita Y., Takegawa K., Shuntoh H., Kuno T.;
RT "Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively
RT regulate cell morphogenesis in fission yeast: the importance of Mn2+
RT homeostasis.";
RL Genes Cells 9:71-82(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Transports calcium and manganese ions into the cell.
CC Regulates cell morphogenesis through control of manganese and calcium
CC homeostasis. {ECO:0000269|PubMed:14723709,
CC 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: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15470240}; Multi-pass membrane protein
CC {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; AC004698; AAC16669.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB39136.1; -; Genomic_DNA.
DR PIR; T40199; T40199.
DR RefSeq; NP_595098.1; NM_001021005.2.
DR AlphaFoldDB; O59868; -.
DR SMR; O59868; -.
DR BioGRID; 276912; 47.
DR STRING; 4896.SPBC31E1.02c.1; -.
DR TCDB; 3.A.3.2.34; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; O59868; -.
DR MaxQB; O59868; -.
DR PaxDb; O59868; -.
DR PRIDE; O59868; -.
DR EnsemblFungi; SPBC31E1.02c.1; SPBC31E1.02c.1:pep; SPBC31E1.02c.
DR GeneID; 2540383; -.
DR KEGG; spo:SPBC31E1.02c; -.
DR PomBase; SPBC31E1.02c; pmr1.
DR VEuPathDB; FungiDB:SPBC31E1.02c; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_1_1; -.
DR InParanoid; O59868; -.
DR OMA; GVHRMAK; -.
DR PhylomeDB; O59868; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O59868; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0015410; F:ABC-type manganese transporter activity; TAS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISO:PomBase.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISO:PomBase.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IGI:PomBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071421; P:manganese ion transmembrane transport; IMP:PomBase.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0061454; P:release of sequestered calcium ion into cytosol by Golgi; IGI: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; IPR006413; P-type_ATPase_IIA_PMR1.
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; TIGR01522; ATPase-IIA2_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; Endoplasmic reticulum;
KW Ion transport; Manganese; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..899
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000046229"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 329
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 899 AA; 98359 MW; 7E45E9180F36FD44 CRC64;
MSVQYDAFSV EQTCADLETD MYNGLSSLQE ITRRNKVHGD NDLKVEDEEN MVVQFLKQFV
KDPLILLLFA SSAISVTLGN IDDAISIALA IVIVVTVGFV QEYRSEQSLK ALNNLVPHYC
NVIRSGKTEH IVASKLVPGD LVILQIGDRV PADLRIVEAT ELEIDESNLT GENSPRKKSS
EAISSNISLT ERNNIAFMGT LVRHGHGRGI VVATGSDTEF GRVFLTMQQT EKPKTPLQNS
MDDLGKQLSL ISLIGIAVIV LVGFFQGKNW LEMLTIGVSL AVAAIPEGLP IIVTVTLALG
VLRMSKKRAI IRRLPSVETL GSVNVICSDK TGTLTMNHMT VTKIYTCGML AAFSLPESEH
IELSVRRTVG IEKALLAAAL CNNSKVHNKA DSILDTTCPW AGFPVDVALI ECSERFGLKD
PRETYSRISE VSFSSERKYM SVAVQYNSSK MNFMKGATEQ VLSSCAYFSD QDGVQHELTA
EMKENIQRNE FEMAASGLRI IAVASGINTN KLVFHGLFGI NDPPRPQVRE SVQYLMTGGV
RVIMITGDSV VTAISIARSL GMAIPSNDEE AIRNYALTGA QLDDLDSSSL RDAVSRVVVF
ARTTPQHKMK IVEALQSLGD VVAMTGDGVN DAPALKLADI GIAMGRQGTD VAKEAADMIL
TDDSFATILS AVEEGKGIFN NIKNFITFQL STSVAALSLI AISSVFGFQN PLNAMQILWI
NILMDGPPAQ SLGVESVDED VMMKPPRPRN APIISVQLLQ RVLLSAFIIV TVTIVVFRVQ
MQDGNVTARD TTMTFTCFVF FDMFNALACR SETKSVFKLG IFSNRMFNIA VGGSLIGQAL
VVYASPFQRI FQTEAIGLKD VLILLACTSS VLWVDEIRKW YRRRKGLVRT KSNYLLRNV
