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Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2 )-ATPase 1) (EC 3.6.3.8) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2 ) ATPase)

 AT2A1_RAT               Reviewed;         994 AA.
Q64578;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1;
Short=SERCA1;
Short=SR Ca(2+)-ATPase 1;
EC=3.6.3.8;
AltName: Full=Calcium pump 1;
AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform;
AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
Name=Atp2a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD Charles River; TISSUE=Skeletal muscle;
PubMed=8447366;
Wu K.D., Lytton J.;
"Molecular cloning and quantification of sarcoplasmic reticulum
Ca(2+)-ATPase isoforms in rat muscles.";
Am. J. Physiol. 264:C333-C341(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-994.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=10329971;
Peters D.G., Mitchell-Felton H., Kandarian S.C.;
"Unloading induces transcriptional activation of the
sarco(endo)plasmic reticulum Ca2+-ATPase 1 gene in muscle.";
Am. J. Physiol. 276:C1218-C1225(1999).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-441; THR-569; SER-581
AND SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Key regulator of striated muscle performance by acting
as the major Ca(2+) ATPase responsible for the reuptake of
cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the
hydrolysis of ATP coupled with the translocation of calcium from
the cytosol to the sarcoplasmic reticulum lumen. Contributes to
calcium sequestration involved in muscular excitation/contraction.
{ECO:0000250|UniProtKB:Q8R429}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2).
-!- ENZYME REGULATION: Inhibited by sarcolipin (SLN), phospholamban
(PLN) and myoregulin (MRLN) (By similarity). Reversibly inhibited
by phospholamban (PLN) at low calcium concentrations (By
similarity). Dephosphorylated PLN decreases the apparent affinity
of the ATPase for calcium. This inhibition is regulated by the
phosphorylation of PLN (By similarity). Enhanced by DWORF; DWORF
increases activity by displacing sarcolipin (SLN), phospholamban
(PLN) and myoregulin (MRLN) (By similarity).
{ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429}.
-!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (By similarity). Interacts with
myoregulin (MRLN). Interacts with DWORF (By similarity).
{ECO:0000250|UniProtKB:Q8R429}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Skeletal muscle, fast twitch muscle (type II)
fibers.
-!- INDUCTION: Increased contractile activity leads to a decrease in
SERCA1 expression, while decreased contractile activity leads to
an increase in SERCA1 expression.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIA subfamily. {ECO:0000305}.
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EMBL; M99223; AAA40991.1; -; mRNA.
EMBL; AF091853; AAD17802.1; -; Genomic_DNA.
EMBL; AF091852; AAD17801.1; -; Genomic_DNA.
PIR; A48849; A48849.
RefSeq; NP_478120.1; NM_058213.1.
UniGene; Rn.217139; -.
UniGene; Rn.3228; -.
ProteinModelPortal; Q64578; -.
SMR; Q64578; -.
BindingDB; Q64578; -.
ChEMBL; CHEMBL3585236; -.
iPTMnet; Q64578; -.
PhosphoSitePlus; Q64578; -.
SwissPalm; Q64578; -.
PRIDE; Q64578; -.
GeneID; 116601; -.
KEGG; rno:116601; -.
CTD; 487; -.
RGD; 621293; Atp2a1.
HOVERGEN; HBG105648; -.
InParanoid; Q64578; -.
KO; K05853; -.
PhylomeDB; Q64578; -.
PRO; PR:Q64578; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
GO; GO:0031673; C:H zone; ISS:UniProtKB.
GO; GO:0031674; C:I band; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:RGD.
GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; IDA:RGD.
GO; GO:0006816; P:calcium ion transport; IDA:RGD.
GO; GO:0045988; P:negative regulation of striated muscle contraction; ISS:UniProtKB.
GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; ISS:UniProtKB.
GO; GO:0006937; P:regulation of muscle contraction; TAS:RGD.
GO; GO:0006942; P:regulation of striated muscle contraction; ISS:UniProtKB.
GO; GO:0043434; P:response to peptide hormone; IDA:UniProtKB.
GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IDA:RGD.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005782; P-type_ATPase_IIA.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Calcium; Calcium transport; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Hydrolase; Ion transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 994 Sarcoplasmic/endoplasmic reticulum
calcium ATPase 1.
/FTId=PRO_0000046190.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.
TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 70 89 Lumenal. {ECO:0000250}.
TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.
TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 274 295 Lumenal. {ECO:0000250}.
TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 314 757 Cytoplasmic. {ECO:0000250}.
TRANSMEM 758 777 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 778 787 Lumenal. {ECO:0000250}.
TRANSMEM 788 808 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 809 828 Cytoplasmic. {ECO:0000250}.
TRANSMEM 829 851 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 852 897 Lumenal. {ECO:0000250}.
TRANSMEM 898 917 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 918 930 Cytoplasmic. {ECO:0000250}.
TRANSMEM 931 949 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 950 964 Lumenal. {ECO:0000250}.
TRANSMEM 965 985 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 986 994 Cytoplasmic. {ECO:0000250}.
REGION 370 400 Interaction with phospholamban 1.
{ECO:0000250|UniProtKB:P04191}.
REGION 788 808 Interaction with phospholamban 2.
{ECO:0000250|UniProtKB:P04191}.
ACT_SITE 351 351 4-aspartylphosphate intermediate.
{ECO:0000250|UniProtKB:P04191}.
METAL 304 304 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 305 305 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 307 307 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 309 309 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 703 703 Magnesium. {ECO:0000250}.
METAL 707 707 Magnesium. {ECO:0000250}.
METAL 768 768 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 771 771 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 796 796 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 800 800 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 800 800 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 908 908 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 569 569 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
DISULFID 876 888 {ECO:0000250|UniProtKB:P04191}.
SEQUENCE 994 AA; 109409 MW; 899F91AD8038A47A CRC64;
MEAAHSKSTE ECLSYFGVSE TTGLTPDQVK RHLEKYGPNE LPAEEGKSLW ELVVEQFEDL
LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAV GIVATTGVST EIGKIRDQMA
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCKMFIID KVDGDICSLN EFSITGSTYA PEGEVLKNDK PVRAGQYDGL VELATICALC
NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR SLSKVERANA CNSVIRQLMK
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP
VKEKIMSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SAKFMEYEMD LTFVGVVGML
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFSENEEVAD RAYTGREFDD
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI
GGYVGAATVG AAAWWFLYAE DGPHVSYHQL THFMQCTEHN PEFDGLDCEV FEAPEPMTMA
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLR
ALDFTQWLMV LKISLPVIGL DELLKFIARN YLEG


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