ID A0A286ZQ54_PIG Unreviewed; 1020 AA.
AC A0A286ZQ54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2A3 {ECO:0000313|Ensembl:ENSSSCP00000033739.1,
GN ECO:0000313|VGNC:VGNC:85648};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000033739.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000033739.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000033739.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000033739.1}
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 -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. Transports calcium ions from
CC the cytosol into the sarcoplasmic/endoplasmic reticulum lumen.
CC Contributes to calcium sequestration involved in muscular
CC excitation/contraction. {ECO:0000256|ARBA:ARBA00002367}.
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|ARBA:ARBA00024147};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000256|ARBA:ARBA00024147};
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|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}.
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DR AlphaFoldDB; A0A286ZQ54; -.
DR SMR; A0A286ZQ54; -.
DR STRING; 9823.ENSSSCP00000033739; -.
DR Ensembl; ENSSSCT00000061709.2; ENSSSCP00000033739.1; ENSSSCG00000017874.5.
DR VGNC; VGNC:85648; ATP2A3.
DR GeneTree; ENSGT00940000155668; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Bgee; ENSSSCG00000017874; Expressed in blood and 42 other cell types or tissues.
DR ExpressionAtlas; A0A286ZQ54; baseline and differential.
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:0030899; F:calcium-dependent ATPase activity; IEA:Ensembl.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF6; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 3; 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 SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000008227};
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 81..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 313..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 781..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 814..833
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 854..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 953..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 61..93
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 805..1008
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 1020 AA; 111452 MW; F27A4DE470CC7C76 CRC64;
MKDELRPQRV SSSSLTAEPW KILCSQLLAS CLQDLGPSGQ AHSCLDAVVP TLSLTPPGKQ
ELPTEEGKSL WELVLEQFED LLVRILLLAA LVSFVLACFE EGEETTTAFV EPLVIVLILV
ANAVVGVWQE RNAENAIEAL KEYEPEMGKV IRSDRKGVQR IRARDIVPGD IVEVAVGDKV
PADLRLIEIK STTLRVDQSI LTGESVSVTK HTDAIPDPRA VNQDKKNMLF SGTNIASGKA
VGVAVATGLH TELGKIRNQM ASVEPERTPL QQKLDEFGRQ LSRAISVICM AVWVINIGHF
ADPAHGGSWL RGAVYYFKIA VALAVAAIPE GLPAVITTCL ALGTRRMARK NAIVRSLPSV
ETLGCTSVIC SDKTGTLTTN QMSVCRMFVV AEAEAGTCRL HEFTISGTTY APEGEVRQGE
QPVRCGKFDG LVELATICAL CNDSALDYNE AKGVYEKVGE ATETALTCLV EKMNVFDTDL
QALSRVERAG ACNAVIKQLM RKEFTLEFSR DRKSMSVYCT PTRPGLVAQG SKMFVKGAPE
SVIERCSSVR VGSRTVPLNT TSREQILAKV RDWGSGSDTL RCLALATRDA PPRKEAMQLD
DCSKFVQYET DLTFVGCVGM LDPPRPEVAS CIARCRQAGI RVVMITGDNK GTAVAICRRL
GILEDTEDVV GKAYTGREFD DLSPEQQRHA CRTARCFARV EPAHKSRIVE NLQSFNEVTA
MTGDGVNDAP ALKKAEIGIA MGSGTAVAKS AAEMVLSDDN FASIVAAVEE GRAIYSNMKQ
FIRYLISSNV GEVVCIFLTA ILGLPEALIP VQLLWVNLVT DGLPATALGF NPPDLDIMEK
RPRNPREALI SGWLFFRYLA IGVYVGLATV AAATWWFLYD AEGPQVTFYQ LRNFLKCSED
NPLFTGTDCE VFESRFPTTM ALSVLVTTEM CNALNSVSEN QSLLRMPPWL NPWLLAAVAM
SMALHFLILL VPPLPLIFQV TPLSGRQWVV VLQISLPVIL LDEALKYLSR KHVDEEKGRQ
//