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Entry: A0A5C6PJ50_9TELE
LinkDB: A0A5C6PJ50_9TELE
Original site: A0A5C6PJ50_9TELE 
ID   A0A5C6PJ50_9TELE        Unreviewed;       921 AA.
AC   A0A5C6PJ50;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=D4764_10G0008540 {ECO:0000313|EMBL:TWW79824.1};
OS   Takifugu flavidus (sansaifugu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW79824.1, ECO:0000313|Proteomes:UP000324091};
RN   [1] {ECO:0000313|EMBL:TWW79824.1, ECO:0000313|Proteomes:UP000324091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW79824.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TWW79824.1};
RA   Xiao S.;
RT   "Chromosome genome assembly for Takifugu flavidus.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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         Evidence={ECO:0000256|RuleBase:RU361146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC         Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC         Evidence={ECO:0000256|ARBA:ARBA00024272};
CC   -!- SUBUNIT: Monomer. Homodimer. {ECO:0000256|ARBA:ARBA00024380}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004205}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004205}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TWW79824.1}.
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DR   EMBL; RHFK02000002; TWW79824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C6PJ50; -.
DR   Proteomes; UP000324091; Chromosome 10.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-EC.
DR   GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR   CDD; cd02085; P-type_ATPase_SPCA; 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; 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   NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF2; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 1; 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; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324091};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        83..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        107..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        273..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        298..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        779..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        811..828
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        848..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        877..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          29..103
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          189..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  100680 MW;  4F377BE658383E25 CRC64;
     MLKKRELLLS QTRPPGEDEN MVPVLTARKA CELPINEVAC VLQADLQVGL SHQEVGRRRA
     YHGWNEFDIG EEEPLWKKYI AQFKDPLILL LLASAVISVL MHQFDDAISI TVAIIIVVTV
     AFVQEYRSEK SLEELGKLVP PECHCVRDGV LEHLLARELV PGDTVCLSVG ERVPADLRLF
     ESTDLSVDES SLTGETTPCS KNTSPQTGGT NRDVASCSNI AFMGTLVRCG KAKGIVIGTG
     ENSEFGEVFK MMQAEESPKT PLQKSMDLLG KQLSLYSLSI IGVIMLVGWL QGKRILDMFT
     IGVSLAVAAI PEGLPIVVTV TLALGVMRMV KKRAIVKKLP IVETLGCCNV ICSDKTGTLT
     KNEMTVTQMF TSDGLHAEVT GVGYNGAGEV LLDGEVIHGF SCPSVAKIVE AGCVCNDSVI
     RNHTLLGRPT EGALIALAMK MGLESLQQEY VRLEEQPFTS EQKCMAIRCV HRTLRDNPGF
     FFMKGAFEQV IRLCTSYNSR GSTLPLTHQQ RELYQQQVSY MGSAGLRVLA FASGPELGNL
     TFLGLVGMID PPRSGVKEAV GTLIGSGVAI KMITGDSQET AISIAARLGF YSKGSQCLSG
     DEVDQLDLQQ LSHMVPRIAV FYRASPRHKL KIVKSLQNIG AVVAMTGDGV NDAVALKAAD
     IGVAMGQTGT DVCKEAADMI LVDDDFRTIM SAIEEGKGIY NNIKNFVRFQ LSTSIAALTL
     ISVATLMNFP NPLNAMQILW INIIMDGPPA QSLGVEPVDR DVIRKPPRNV KDSIITRGLI
     LKVLVSAFII VCGTLFVFWR ELQDNMITPR DTTMTFTCFV FFDMFNALSS RSQTRMVHEM
     GLCSNRTFCY AVLASIMGQL LVIYFPPLQS VFQTESLSLT DLLFLLALTS SVCIVSELIK
     MGERWRGGAN RDLPTDFFHD V
//
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