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Database: UniProt
Entry: A0AAY5JVZ6_ESOLU
LinkDB: A0AAY5JVZ6_ESOLU
Original site: A0AAY5JVZ6_ESOLU 
ID   A0AAY5JVZ6_ESOLU        Unreviewed;      1000 AA.
AC   A0AAY5JVZ6;
DT   05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2025, sequence version 1.
DT   28-JAN-2026, entry version 5.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000080544.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000080544.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Myers G., Karagic N., Meyer A., Pippel M., Reichard M., Winkler S.,
RA   Tracey A., Sims Y., Howe K., Rhie A., Formenti G., Durbin R., Fedrigo O.,
RA   Jarvis E.D.;
RT   "Esox lucius (northern pike) genome, fEsoLuc1, primary haplotype.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000080544.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSELUP00000080544.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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}.
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DR   RefSeq; XP_034149026.1; XM_034293135.1.
DR   AlphaFoldDB; A0AAY5JVZ6; -.
DR   Ensembl; ENSELUT00000108805.1; ENSELUP00000080544.1; ENSELUG00000020396.3.
DR   GeneID; 105025950; -.
DR   GeneTree; ENSGT00940000155668; -.
DR   Proteomes; UP000265140; Chromosome 7.
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; 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; 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   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:UP000265140};
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..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        292..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        758..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        831..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        926..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        960..978
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   1000 AA;  109922 MW;  D2FFF5A85B30D207 CRC64;
     MDSAHTKPAS EVLENFGVNE NTGLTLDQVK SNFEKYGPNE LPAEEGKSLW ELVVEQFEDL
     LVRILLLAAC VSFVLALFEE GEETVTAFVE PFVILLILIA NAVIGVWQER NAENAIEALK
     EYEPEIAKVY RMNRKAVQRI KARELVPGDI VEIAVGDKVP ADIRITSIKS TTLRVDQSIL
     TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGRAV GMVVATGVST EIGKIRNQMA
     STEQEKTPLQ QKLDEFGEQL SKVISLICVA VWVINIGHFG DPVHGGSWMR GAVYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVCRMFVVD KVEDSSCALH EFSITGSTYA PEGQVLKDDR VVQCADYDGL LELATVCSMC
     NDSSLDYNEA KGVYEKVGEA TETALTTLVE KMNVFKTDVS GLSKVERAGA CNSVIKQLMS
     KEFTLEFSRD RKSMSVYCTP TSKTGSGSKM FVKGAPESVM ERCQYLRVGT GKVPLTLPLR
     EQLTATIRDW GTGRDTLRCL GMATRDTPPK PEDMDLENSA KFADYETGLT FVGCVGMLDP
     PRKEVIGSIK LCAEAGIRVI MITGDNKCTA VAICRRIGIF REDEDVAGKA YTGREFDDLP
     LEAQRDAVKR ARCFARVEPA HKSKIVGFLQ SFDEITAMTG DGVNDAPALK KAEIGIAMGS
     GTAVAKSASE MVLSDDNFST IVAAVEEGRA IYNNMKQFIR YLISSNVGEV VCIFLTAILG
     LPEALIPVQL LWVNLVTDGL PATALGFNPP DLDIMDKPPR NPKEPLISGW LFFRYLAIGG
     YVGLGTVGAA TWWYLFDDAG PQVSFYQLRH FMQCTEDNPM FQGVDCEVFE SRYPTTMALS
     VLVTIEMFNS LNSLSENQSL IRMPPWVNFW LLGAIILSLS LHFLILYVEP LPLIFQVTPL
     NWYQWIVVLK ISIPVILLDE ALKYLSRNHL DDNEDKRGSR
//
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