AT2A3_CHICK
ID AT2A3_CHICK Reviewed; 999 AA.
AC Q9YGL9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
DE Short=ChkSERCA3;
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SERCA3A AND SERCA3B).
RC STRAIN=SPAFAS; TISSUE=Macrophage;
RX PubMed=10413590; DOI=10.1006/excr.1999.4526;
RA Machuca I., Domenget C., Jurdic P.;
RT "Identification of avian sarcoplasmic reticulum Ca(2+)-ATPase (SERCA3) as a
RT novel 1,25(OH)(2)D(3) target gene in the monocytic lineage.";
RL Exp. Cell Res. 250:364-375(1999).
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).
CC {ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SERCA3A;
CC IsoId=Q9YGL9-2; Sequence=Displayed;
CC Name=SERCA3B;
CC IsoId=Q9YGL9-1; Sequence=VSP_060853;
CC -!- TISSUE SPECIFICITY: Found in spleen, lung, intestine and brain.
CC -!- INDUCTION: Down-regulated by 1,25-dihydroxyvitamin D3.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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 EMBL; Y18063; CAB38029.1; -; mRNA.
DR RefSeq; NP_990222.1; NM_204891.1. [Q9YGL9-1]
DR AlphaFoldDB; Q9YGL9; -.
DR SMR; Q9YGL9; -.
DR STRING; 9031.ENSGALP00000002373; -.
DR PaxDb; Q9YGL9; -.
DR GeneID; 395707; -.
DR KEGG; gga:395707; -.
DR CTD; 489; -.
DR VEuPathDB; HostDB:geneid_395707; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; Q9YGL9; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q9YGL9; -.
DR PRO; PR:Q9YGL9; -.
DR Proteomes; UP000000539; Unplaced.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
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_0000046206"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 314..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 758..777
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 778..787
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 788..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 809..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 829..851
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 852..897
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 898..917
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 918..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 931..949
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 950..964
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 965..985
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 986..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
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="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 796
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 908
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT VAR_SEQ 995..999
FT /note="EEDKK -> ILRTVRNTWSGEHQLKTCRTPEQGRRGQEMNDTKEMLQAKGPQ
FT TCNSD (in isoform SERCA3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_060853"
SQ SEQUENCE 999 AA; 110546 MW; 53A3FFE8CEFC54CE CRC64;
MEAAHSVPVQ DVLSRFGVAE SCGLSPEQVR RNREKYGPNE LPAEERKSLW ELVLEQFEDL
LVRILLMAAF LSFILAWFEE GEESTTAFVE PIVIIMILIA NAVVGVWQER NAESAIEALK
EYEPEMGKVI RADRSGVQRI RARDIVPGDI VEVAVGDKVP ADIRIIEIRS TTLRVDQSIL
TGESMSVIKH ADPIPDPRAV NQDKKNMLFS GTNIAAGKAV GIVIATGVYT EIGKIRNQMV
ETEPEKTPLQ QKLDEFSQQL SKVIFLVCIA VWVINISHFS DPVHGGSWFR GAIYYFKTSV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFIME KVEGTQCSLH EFSITGSTYA PEGQILKDEK PVRCGQYDGL VELATICALC
NDSSLDYNES KKVYEKVGEA TETALTCLVE KMNVFDTDTS KLSKVERANA CNSVIKHLMR
KECTLEFSRD RKSMSVYCTP TGPGHNSAGS KMFVKGAPES VIERCTHVRV GTAKVPLTPP
VREKILSQIR DWGMGTDTLR CLALATHDAP VQRETMQLHD STTFTHYETN LTFVGCVGML
DPPRKEVTSS IEMCRKAGIR VIMITGDNKG TAVAICRRIG IFTESEDVAG KAYTGREFDE
LSPEAQRQAC REARCFARVE PAHKSRIVEY LQSFNEITAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKSA AEMVLSDDNF STIVSAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAI
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDKL PRNPKEPLIS GWLFFRYLAI
GVYVGLATVG AATWWFLYDA EGPQVSFHQL RNFMRCTEDN PIFEGVNCEI FESRYPTTMA
LSVLVTIEMC NALNSVSENQ SLLRMPPWLN IWLLGAIVMS MALHFFILYV KPMPLIFQVT
PLSWPQWVVV LKISLPVILL DEGLKYLSRN HLEGEEDKK
