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Database: UniProt
Entry: A0A9D3RIL0_ANGAN
LinkDB: A0A9D3RIL0_ANGAN
Original site: A0A9D3RIL0_ANGAN 
ID   A0A9D3RIL0_ANGAN        Unreviewed;       994 AA.
AC   A0A9D3RIL0;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=ANANG_G00286150 {ECO:0000313|EMBL:KAG5831971.1};
OS   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936 {ECO:0000313|EMBL:KAG5831971.1, ECO:0000313|Proteomes:UP001044222};
RN   [1] {ECO:0000313|EMBL:KAG5831971.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tag_6206 {ECO:0000313|EMBL:KAG5831971.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:KAG5831971.1};
RA   Henkel C., Jong-Raadsen S.A., Dufour S., Weltzien F.-A., Palstra A.P.,
RA   Pelster B., Spaink H.P., Van Den Thillart G.E., Jansen H., Zahm M.,
RA   Klopp C., Cedric C., Louis A., Berthelot C., Parey E., Roest Crollius H.,
RA   Montfort J., Robinson-Rechavi M., Bucao C., Bouchez O., Gislard M.,
RA   Lluch J., Milhes M., Lampietro C., Lopez Roques C., Donnadieu C.,
RA   Braasch I., Desvignes T., Postlethwait J., Bobe J., Guiguen Y., Dirks R.;
RT   "A chromosome-scale assembly of European eel, Anguilla anguilla.";
RL   Submitted (JAN-2021) 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=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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|ARBA:ARBA00047282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000256|ARBA:ARBA00047282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004326}.
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:KAG5831971.1}.
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DR   EMBL; JAFIRN010000017; KAG5831971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9D3RIL0; -.
DR   Proteomes; UP001044222; Chromosome 17.
DR   GO; GO:0033017; C:sarcoplasmic reticulum 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   CDD; cd02083; P-type_ATPase_SERCA; 1.
DR   FunFam; 3.40.1110.10:FF:000003; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000005; Calcium-transporting ATPase 1; 1.
DR   FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 3.
DR   FunFam; 2.70.150.10:FF:000160; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 2.
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; 2.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001044222};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        60..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        84..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        260..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        298..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        760..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        833..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        931..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          3..77
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   994 AA;  108746 MW;  D3F13A33823B1D51 CRC64;
     MENAHTKEPA ECLAHFSVSE ATGLTPDQFQ KNLEKFGYNE LPAEEGKSIW ELVAEQFEDL
     LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAVVGVWQER NAEDAIEALK
     EYEPEMGKVY RADRKSVQRI KAREIVPGDV VEVSVGDKVP ADIRITAIRS TTLRVDQSIL
     TGESVSVIKH TEAVPDPRAV NQDKKNMLFS GTNIAAGRAI GVAVATGVAT EIGKIRDQMA
     ATEQEKTPLQ QKLDEFGEQL SKVISLICVA VWMINIGHFN DPVHGGSWIR GAVYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MCVTKMFVIE KVEDENVVLD EFNISGSKYT PEGEVSKGSA LVQCSQYDGL VELATICALC
     NDSSLDFNES KGIYEKVGEA TETALCCLVE KMNVFGTEVR GLSKVERANT CCSVIKQLMK
     KEFTLEFSRD RKSMSVYCSP AKASKAPVGN KMFVKGAPEG VIDRCAYVRV GTTRVPLTGP
     VKDKIMTIIK EWGTGRDTLR CLALATRDNP LKPEEMNLED STKFADYETD LTFVGCVGML
     DPPRKEVVGS IELCRAAGIR VIMITGDNKG TAVAICRRIG IFGEDEDVTG RAFTGREFDD
     LPIEAQRDAV RKACCYARVE PSHKSKIVEF LQSFDEITAM TGDGVNDAPA LKKAEIGIAM
     GSGTAVAKSA SEMVLADDNF SSIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA
     LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMGKA PRSPKEPLIS GWLFFRYMAI
     GGYVGAATVA AAAWWFLYAD DGPAVSYYQL SHFMQCHDEN EDFAGIECEV FEASPPMTMA
     LSVLVTIEMC NALNSLSENQ SLVRMPPWSN GWLVGAMTLS MSLHFMIIYV DPLPMVFKLT
     HLNLEQWIVV LKLSFPVILI DEVLKFVARN YLEA
//
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