Atp2a1
entrez
11937
canonical
uniprot
Q8R429
canonical
ensembl
ENSMUSG00000030730
resolver
ensp
ENSMUSP00000032974
resolver
enst
ENSMUST00000032974
resolver
genesymbol
Atp2a1
resolver
uniprot_entry
AT2A1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (PubMed:21697544, PubMed:22961106, PubMed:25640239). Has also been shown to be reversibly inhibited by phospholamban (PLN) at low calcium concentrations in vitro (By similarity). Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium in vitro and 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) (PubMed:26816378). {ECO:0000250|UniProtKB:P04191, ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106, ECO:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378}.
uniprot
proteins
amino_acid_sequence
MEAAHSKSTEECLSYFGVSETTGLTPDQVKRHLEKYGPNELPAEEGKSLWELVVEQFEDLLVRILLLAACISFVLAWFEEGEETVTAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAVGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDVCSLNEFSITGSTYAPEGEVLKNDKPVRAGQYDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRSLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGPVKEKIMSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSAKFMEYEMDLTFVGVVGMLDPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFSENEEVTDRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFLYAEDGPHVSYHQLTHFMQCTEHNPEFDGLDCEVFEAPEPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLRALDFTQWLMVLKISLPVIGLDELLKFIARNYLEG
uniprot
proteins
ec_number
7.2.2.10
uniprot
proteins
function
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 (PubMed:21697544, PubMed:22961106, PubMed:25640239, PubMed:26816378, PubMed:27923914). 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 (PubMed:21697544, PubMed:22961106, PubMed:25640239, PubMed:26816378). {ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106, ECO:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378, ECO:0000269|PubMed:27923914}.
uniprot
proteins
mass_dalton
109425
uniprot
proteins
mutagenesis
MUTAGEN 795; /note="V->A: Impaired interaction with DWORF and PLN; when associated with A-802 and A-809."; /evidence="ECO:0000269|PubMed:26816378"; MUTAGEN 802; /note="L->A: Impaired interaction with DWORF and PLN; when associated with A-795 and A-809."; /evidence="ECO:0000269|PubMed:26816378"; MUTAGEN 809; /note="F->A: Impaired interaction with DWORF and PLN; when associated with A-796 and A-802."; /evidence="ECO:0000269|PubMed:26816378
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IIA subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21697544
uniprot
proteins
pubmed
22961106
uniprot
proteins
pubmed
25640239
uniprot
proteins
pubmed
26816378
uniprot
proteins
pubmed
27923914
uniprot
proteins
sequence_length
994
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}.
uniprot
proteins
transmembrane_region
TRANSMEM 49..69; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 90..110; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 254..273; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 296..313; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 758..777; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 788..808; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 829..851; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 898..917; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 931..949; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 965..985; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P04191
uniprot
proteins