ID   ATC1_DUNBI              Reviewed;        1037 AA.
AC   P54209;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Cation-transporting ATPase CA1;
DE            EC=7.2.2.-;
GN   Name=CA1;
OS   Dunaliella bioculata (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX   NCBI_TaxID=13790;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SAG 19-4;
RX   PubMed=8987619; DOI=10.1007/bf00196652;
RA   Raschke B.C., Wolf A.H.;
RT   "Molecular cloning of a P-type Ca(2+)-ATPase from the halotolerant alga
RT   Dunaliella bioculata.";
RL   Planta 200:78-84(1996).
CC   -!- FUNCTION: Could possibly be a calcium ATPase.
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 IIA subfamily. {ECO:0000305}.
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DR   EMBL; X93592; CAA63790.1; -; mRNA.
DR   AlphaFoldDB; P54209; -.
DR   SMR; P54209; -.
DR   PRIDE; P54209; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
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; IPR005782; P-type_ATPase_IIA.
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; TIGR01116; ATPase-IIA1_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1037
FT                   /note="Cation-transporting ATPase CA1"
FT                   /id="PRO_0000046241"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        731..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        790..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        852..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        945..965
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        971..991
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        370
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1037 AA;  111801 MW;  18100AC444F1EA87 CRC64;
     MVSHASSGRP SSRDTGMVYL GLGMQDAYSS EVQEVAAFYH VDLDRGLSDR DVQQARIKYG
     RNQMEAEQST PLWKLILKQF DDLLVKILLG AAIVDFIIAI SEGESIQSGL IEPMVILLIL
     VANATVGVVT ERNAEKAIEQ LKSYEADDAT VLRNGQLQLI PSADIVPGDI VELAVGNKVP
     ADTRVSHIYT TSLKIDQSLL TGESQAVEKH TEVVHNEQAV YQDKLNMLFS GTLVVAGRAR
     GIVVGTGSNT AIGKIRDAMG VEEDVVTPLK AKLDEFGALL SKVIAGICVL VWVVNINRFN
     DPALGGWFQG AIHYFKIAVA LAVAAIPEGL PAVVTTCLAL GTRKMARHNA IVRTLPSVET
     LGCTTVICSD KTGTLTTNQM SVIKVAAVQS SSSQLAEFDV TGTTFSPEGM VLGPGGVVLR
     QPADTPCLAH AAQCAALCND SQVFVAQKTG TLQRIGESTE IALRVFAEKI GLPSSIRPDR
     PISRSQFGTN NFWQEDVERL ALLEFSRDRK MMSVLVKGSD RQHNIWSKGA PEFVLRKCSH
     VLANNGEGAV PLTDNMRQAI LSDMQAFGSR QALRCLALAF KSVPTTTTKL DYSDESGLTF
     IGLLGMHDPP RPECRSALST CHNAGIKVIM VTGDNKGTAE AVARQVGALS PSTALAGSDD
     EDNLGISYTG REFEEMGALG QAAATRNLVV LSRVEPMHKL RLVELLKAQG HVVAMTGDGV
     NDAPALLRAD IGIAMGSGTA VAKHAADMVL GDDNFATIVF AVAEGRVIFN NTKQFIRYMI
     SSNIGEVVAI FLAALLGLPE VLTPVQLLWV NLVTDGLPAT ALGFNRADKD MMARGPRRVD
     DPIVNGWLFL RYLIIGMYVG IVTVYGFIWW YISFPEGGNM TWSQLTHFQA CASQPGGAKD
     CEVFHSKHPT TISMSVLVVV EMFNALNNLS EDSSLLRIPP WDNKWLVGAI ATSMALHFGI
     LYTGASAMFG VTGLSFAEWT MVIKLSAPVI LVDEIMKAWS RRRQRHPASS RGGPVSLMEI
     QVPLTSSSRD EAALKLK