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Database: UniProt
Entry: A0AA88NEE9_TACVA
LinkDB: A0AA88NEE9_TACVA
Original site: A0AA88NEE9_TACVA 
ID   A0AA88NEE9_TACVA        Unreviewed;      1065 AA.
AC   A0AA88NEE9;
DT   27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT   27-MAR-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=Q7C36_007596 {ECO:0000313|EMBL:KAK2852395.1};
OS   Tachysurus vachellii (Darkbarbel catfish) (Pelteobagrus vachellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Bagridae; Tachysurus.
OX   NCBI_TaxID=175792 {ECO:0000313|EMBL:KAK2852395.1, ECO:0000313|Proteomes:UP001187315};
RN   [1] {ECO:0000313|EMBL:KAK2852395.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PRFRI_2022a {ECO:0000313|EMBL:KAK2852395.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAK2852395.1};
RA   Liu H.;
RT   "Pelteobagrus vachellii genome.";
RL   Submitted (AUG-2023) 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|RuleBase:RU361146};
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:KAK2852395.1}.
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DR   EMBL; JAVHJS010000007; KAK2852395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AA88NEE9; -.
DR   Proteomes; UP001187315; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02083; P-type_ATPase_SERCA; 1.
DR   FunFam; 2.70.150.10:FF:000143; Calcium-transporting ATPase; 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   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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001187315};
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        767..788
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        800..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        840..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        939..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1036..1055
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   1065 AA;  117408 MW;  26412E497968E311 CRC64;
     MDNAHTKTVE EVLGFFGVNE STGLSSEHLR KNRERWGPNE LPAEEGKSLW ELVLEQFEDL
     LVRILLLAAC ISFTLAWFEE GEGTITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
     EYEPEMGKVY RQDKKSVQRV RARDIVPGDI VEVAVGDKVP ADIRLTSIRS TTLRVDQSIL
     TGESVSVLKH TDPVPDPRAV NQDKKNMLFS GTNIAAGRAI GVVVATGVQT EIGKIRDEMA
     ATDPERTPLQ QKLDQFGEQL SKVITVICVA VWGINIGHFN DPVHGGSWLR GAVYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVCRMFVVE KVKDERCVLN EFTVTGSTYA PEGEVYRNDS VVRCSQYDAL VEMATICALC
     NDSSLDYNES KGVYEKVGEA TETALCCLVE KMNVFDTDLR SLIPVERATA CCSVIKQLMR
     KDLTLEFSRD RKSMSVFCSP NKLARSATGA KMFVKGAPEN VLERCRWIRI GGGARIPMTS
     DLREHLLGTV REWSSGRDTL RCLAMATRDS PPDPRTLNLE NSSAFSEYES ELTFVGCVGM
     LDPPRKEVLN AVRMCRQAGI RVIMITGDNK GTALSICRRV GIITEQEEEE AEGTPFGGGL
     TGREFDELPP HLQRQACRTT RCFARVEPTH KSRIVEYLQS LSDITAMTGD GVNDAPALKK
     AEIGIAMGSG TAVAKSASEM ILADDNFSTI VAAVEEGRAI YNNMKQFIRY LISSNIGEVV
     CIFLTAALGM PEALIPVQLL WVNLVTDGFP ATALGFNPPD LDIMSRPPRS PKEPLISGWL
     FCRYLIIGCY VGVATVGAAA WWFMAAHDGP KLSFYQLSHY MQCSEGHADF AGVQCSVFES
     PYPMTMALSV LVTIEMCNAL NSLSENQSLL KMPPWSNPWL VGAICLSMAL HFLILYVDPL
     PMIFQIRPLS WPQWVTVLKM SLPVILMDEA LKFLARNYIE PGNDLEQEEE ERLHHGQGSS
     GGFASLAGKI QQGLKGVSWA FVFISAPLLF WIYSLDSDIT NIFWE
//
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