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 02-SEP-2026, entry version 115. 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 + phosphate + H(+); 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}. 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; X93592; CAA63790.1; -; mRNA. DR AlphaFoldDB; P54209; -. DR SMR; P54209; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:InterPro. DR CDD; cd02083; P-type_ATPase_SERCA; 1. DR FunFam; 2.70.150.10:FF:000055; Calcium-transporting ATPase; 1. DR FunFam; 3.40.1110.10:FF:000003; Calcium-transporting ATPase; 1. DR FunFam; 1.20.1110.10:FF:000027; Calcium-transporting ATPase, putative; 1. DR FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 1. DR FunFam; 3.40.50.1000:FF:000083; Sodium/potassium-transporting ATPase subunit alpha; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR059000; ATPase_P-type_domA. 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 NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 3. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF08282; Hydrolase_3; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00120; HATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. 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 //