ID A0A669BLZ2_ORENI Unreviewed; 1001 AA.
AC A0A669BLZ2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=LOC100706607 {ECO:0000313|Ensembl:ENSONIP00000036556.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000036556.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000036556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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=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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
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 ---------------------------------------------------------------------------
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 AlphaFoldDB; A0A669BLZ2; -.
DR Ensembl; ENSONIT00000080064.1; ENSONIP00000036556.1; ENSONIG00000011494.2.
DR GeneTree; ENSGT00940000164922; -.
DR Proteomes; UP000005207; Unplaced.
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 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; 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 PANTHER; PTHR42861:SF92; 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; 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 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:UP000005207};
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}; Transport {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 759..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 832..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 930..949
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 1001 AA; 109905 MW; 59B3DEAE7126B11A CRC64;
MENSHTKTPA ECLAYFSVNE NSGLTPDQFK KNLDKYGFNE LPAEEGKSIW ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAVVGVWQER NAESAIEALK
EYEPEMGKVY RSDRKSVQRI KAREIVPGDI VEVSVGDKVP ADIRIVSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAI GVAVATGVST EIGKIRDQMA
ATEQEKTPLQ AKLDEFGEQL SKVISLICVA VWAINIGHFN DPVHGGSWIR GAVYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MCVTKMFVVK TVDGDHVDLD AFDISGSKYT PEGEVQSNSD KPTLICFSYD GLVELATICA
LCNDSSLDYN ESKKIYEKVG EATETALCCL VEKMNVFNSN VKNLSRIERA NACCTVIKQF
MKKKFTLEFS RDRKSMSVYC TPVKGDGGPK MFVKGAPEGV IDRCAYVRVG TTRVPLTNAI
KEKILSVIRD WGTGRDTLRC LALATRDSPL KVEEMNLEDS TKFADYETDL TFVGCVGMLD
PPRKEVTDSI ELCRAAGIRV IMITGDNKGT AIAICRRIGI FSEDEDVSGR AYTGREFDDL
PLHEQSEAVR RACCFARVEP AHKSKIVEFL QGYDDITAMT GDGVNDAPAL KKAEIGIAMG
SGTAVAKSAS EMVLADDNFS SIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GLPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMGKPP RSPKEPLISG WLFFRYMAIG
GYVGAATVAG AAWWFLYDTT GPGVTYYQLS HFMQCHEENE DFEGLDCEIF EAAPPMTMAL
SVLVTIEMCN ALNSLSENQS LVRMPPWSNF WLISAMTLSM SLHFMIIYVD PLPMIFKLTH
LSTEQWIVVL KLSFPVIAID EVLKFVARNY VEAPHLKCSP L
//
