AT2A3_PIG
ID AT2A3_PIG Reviewed; 999 AA.
AC O77696; A0A286ZW82; K9IW69;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
DE Short=SERCA3;
DE Short=SR Ca(2+)-ATPase 3;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump 3;
GN Name=ATP2A3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 773-907, AND TISSUE SPECIFICITY.
RC TISSUE=Coronary artery;
RX PubMed=10724327; DOI=10.1023/a:1007093516593;
RA Khan I., Sandhu V., Misquitta C.M., Grover A.K.;
RT "SERCA pump isoform expression in endothelium of veins and arteries: every
RT endothelium is not the same.";
RL Mol. Cell. Biochem. 203:11-15(2000).
RN [2] {ECO:0000312|EMBL:JAA53532.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Dawson H.D., Chen C.T.;
RT "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT Sequencing.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:HDB02571.1}
RP IDENTIFICATION.
RX PubMed=30723633; DOI=10.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
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:0000250|UniProtKB:Q93084}.
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:0000250|UniProtKB:Q93084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000250|UniProtKB:Q93084};
CC -!- ACTIVITY REGULATION: Inhibited by sarcolipin (SLN), phospholamban (PLN)
CC and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF
CC increases activity by displacing sarcolipin (SLN), phospholamban (PLN)
CC and myoregulin (MRLN) (By similarity). {ECO:0000250|UniProtKB:P04191,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts
CC with phospholamban (PLN) (By similarity). Interacts with myoregulin
CC (MRLN). Interacts with DWORF (By similarity). Interacts VMP1 (By
CC similarity). Interacts with TUNAR; the interaction occurs at low levels
CC in low glucose conditions and is increased by high glucose levels (By
CC similarity). {ECO:0000250|UniProtKB:P04191,
CC ECO:0000250|UniProtKB:Q8R429, ECO:0000250|UniProtKB:Q93084}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q93084}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q93084}.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial tissues.
CC {ECO:0000269|PubMed:10724327}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; AF084929; AAC33481.1; -; mRNA.
DR EMBL; GACC01000275; JAA53532.1; -; mRNA.
DR EMBL; AEMK02000082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQIR01197659; HDB53136.1; -; Transcribed_RNA.
DR EMBL; DQIR01147094; HDB02571.1; -; Transcribed_RNA.
DR EMBL; DQIR01162709; HDB18186.1; -; Transcribed_RNA.
DR EMBL; DQIR01166546; HDB22023.1; -; Transcribed_RNA.
DR AlphaFoldDB; O77696; -.
DR SMR; O77696; -.
DR STRING; 9823.ENSSSCP00000018933; -.
DR PaxDb; O77696; -.
DR Ensembl; ENSSSCT00000056237; ENSSSCP00000035943; ENSSSCG00000017874.
DR Ensembl; ENSSSCT00055060309; ENSSSCP00055048321; ENSSSCG00055029890.
DR VGNC; VGNC:85648; ATP2A3.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000155668; -.
DR InParanoid; O77696; -.
DR OrthoDB; 100699at2759; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000017874; Expressed in blood and 42 other tissues.
DR ExpressionAtlas; O77696; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Disulfide bond;
KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..999
FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 3"
FT /id="PRO_0000046204"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 70..89
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 274..295
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 314..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 758..777
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 778..787
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 788..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 809..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 829..851
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 852..897
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 898..917
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 918..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 931..949
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 950..964
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 965..985
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 986..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 370..400
FT /note="Interaction with phospholamban 1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT REGION 788..808
FT /note="Interaction with phospholamban 2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 768
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 796
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 908
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q93084"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64518"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64518"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64518"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64518"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93084"
FT DISULFID 876..888
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT CONFLICT 205
FT /note="K -> E (in Ref. 2; JAA53532)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="G -> S (in Ref. 2; JAA53532)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="D -> N (in Ref. 2; JAA53532)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="V -> A (in Ref. 2; JAA53532)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="R -> L (in Ref. 1; AAC33481)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="Y -> H (in Ref. 1; AAC33481)"
FT /evidence="ECO:0000305"
FT CONFLICT 884..886
FT /note="TGT -> AGI (in Ref. 1; AAC33481)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="T -> I (in Ref. 1; AAC33481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 109328 MW; 4D49EEE3510047E1 CRC64;
MEEAHLLPAA DVLRRFSVTA EGGLSPAQVT RARERYGPNE LPTEEGKSLW ELVLEQFEDL
LVRILLLAAL VSFVLACFEE GEETTTAFVE PLVIVLILVA NAVVGVWQER NAENAIEALK
EYEPEMGKVI RSDRKGVQRI RARDIVPGDI VEVAVGDKVP ADLRLIEIKS TTLRVDQSIL
TGESVSVTKH TDAIPDPRAV NQDKKNMLFS GTNIASGKAV GVAVATGLHT ELGKIRNQMA
SVEPERTPLQ QKLDEFGRQL SRAISVICMA VWVINIGHFA DPAHGGSWLR GAVYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFVVA EAEAGTCRLH EFTISGTTYA PEGEVRQGEQ PVRCGKFDGL VELATICALC
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTDLQ ALSRVERAGA CNAVIKQLMR
KEFTLEFSRD RKSMSVYCTP TRPGLVAQGS KMFVKGAPES VIERCSSVRV GSRTVPLNTT
SREQILAKVR DWGSGSDTLR CLALATRDAP PRKEAMQLDD CSKFVQYETD LTFVGCVGML
DPPRPEVASC IARCRQAGIR VVMITGDNKG TAVAICRRLG ILEDTEDVVG KAYTGREFDD
LSPEQQRHAC RTARCFARVE PAHKSRIVEN LQSFNEVTAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKSA AEMVLSDDNF ASIVAAVEEG RAIYSNMKQF IRYLISSNVG EVVCIFLTAI
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKR PRNPREALIS GWLFFRYLAI
GVYVGLATVA AATWWFLYDA EGPQVTFYQL RNFLKCSEDN PLFTGTDCEV FESRFPTTMA
LSVLVTTEMC NALNSVSENQ SLLRMPPWLN PWLLAAVAMS MALHFLILLV PPLPLIFQVT
PLSGRQWVVV LQISLPVILL DEALKYLSRK HVDEEKGRQ
