ATC3_SCHPO
ID ATC3_SCHPO Reviewed; 1037 AA.
AC P22189;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 178.
DE RecName: Full=Calcium-transporting ATPase 3;
DE EC=7.2.2.10;
GN Name=cta3; ORFNames=SPBC24E9.06, SPBC839.06;
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].
RX PubMed=2145281; DOI=10.1016/s0021-9258(17)44766-1;
RA Ghislain M., Goffeau A., Halachmi D., Eilam Y.;
RT "Calcium homeostasis and transport are affected by disruption of cta3, a
RT novel gene encoding Ca2(+)-ATPase in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 265:18400-18407(1990).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012, 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: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of the calcium.
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: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IID subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05634; AAA35290.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB46699.1; -; Genomic_DNA.
DR PIR; A36096; A36096.
DR RefSeq; NP_595246.1; NM_001021152.2.
DR AlphaFoldDB; P22189; -.
DR SMR; P22189; -.
DR BioGRID; 277718; 10.
DR STRING; 4896.SPBC839.06.1; -.
DR TCDB; 3.A.3.9.2; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P22189; -.
DR MaxQB; P22189; -.
DR PaxDb; P22189; -.
DR PRIDE; P22189; -.
DR EnsemblFungi; SPBC839.06.1; SPBC839.06.1:pep; SPBC839.06.
DR GeneID; 2541204; -.
DR KEGG; spo:SPBC839.06; -.
DR PomBase; SPBC839.06; cta3.
DR VEuPathDB; FungiDB:SPBC839.06; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_0_1; -.
DR InParanoid; P22189; -.
DR OMA; RRFLTYH; -.
DR PhylomeDB; P22189; -.
DR PRO; PR:P22189; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IMP:PomBase.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP: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:0097623; P:potassium ion export across plasma membrane; IDA:PomBase.
DR GO; GO:0051208; P:sequestering of calcium ion; IDA:PomBase.
DR CDD; cd02086; P-type_ATPase_Na_ENA; 1.
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; IPR006414; P-type_ATPase_IID.
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; TIGR01523; ATPase-IID_K-Na; 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; Ion transport; Magnesium;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1037
FT /note="Calcium-transporting ATPase 3"
FT /id="PRO_0000046238"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 368
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1037 AA; 115327 MW; 80D2BDF2292CE2B9 CRC64;
MVTINISNPV YFSDIKDVES EFLTSIPNGL THEEAQNRLS EYGENRLEAD SGVSAWKVLL
RQVLNAMCVV LILAAALSFG TTDWIEGGVI SAIIVLNITV GFIQEYKAEK TMDSLRTLAS
PMAHVTRSSK TDAIDSHLLV PGDVVVLKTG DVVPADLRLV ETVNFETDEA LLTGESLPVI
KDAHATFQMN EDVPIGDRIN LAYSSSIVTK GRAKGICYAT GMQTQIGAIA AGLRQKGKLF
QRPEKDEPNY RRKLNKYYLK VTSYYVQRVL GLNVGTPLQR KLTVLAYILF CIAIILAIIV
MAAHSFHVTN EVSIYAISLG ISIIPESLIA VLSITMAMGQ KNMSKRRVIV RKLEALEALG
GVTDICSDKT GTITQGKMIT RRVWIPSYGY LSVDTSDANN PTIGTVSGLE AAMQDVLKEK
KQEMKNIDPS NQPSDQFIPL LKTCALCNLS TVNQTETGEW VVKGEPTEIA LHVFSKRFNY
GKEDLLKTNT FVREYPFDSE IKRMAVIYED QQGQYTVYAK GAVERILERC STSNGSTLEE
PDRELIIAQM ETLAAEGLRV LALATKVIDK ADNWETLPRD VAESSLEFVS LVGIYDPPRT
ESKGAVELCH RAGIRVHMLT GDHPETAKAI AREVGIIPPF ISDRDPNMSW MVMTGSQFDA
LSDEEVDSLK ALCLVIARCA PQTKVKMIEA LHRRKAFVAM TGDGVNDSPS LKQANVGIAM
GQNGSDVAKD ASDIVLTDDN FSSIVNAIEE GRRMFDNIMR FVLHLLVSNV GEVILLVVGL
AFRDEVHLSV FPMSPVEILW CNMITSSFPS MGLGMELAQP DVMERLPHDN KVGIFQKSLI
VDMMVYGFFL GVVSLMTWVV IMYGFGTGNL SYDCNAHYHA GCNDVFKARS AVFAVVTFCI
LIMAVEVKNF DNSLFNLHGI PWGEWNFRYF LHTLVENKFL AWAIALAAVS VFPTIYIPVI
NRDVFKHTYI GWEWGVVAVA VMFYFFYVEI WKSIRRSLTN PQKKGKFRRT LSNTITTESK
LSEKDLEHRL FLQSRRA
