Atp2a2
entrez
29693
canonical
uniprot
P11507
canonical
ensembl
ENSRNOG00000001285
resolver
ensembl
ENSRNOG00055015092
resolver
ensembl
ENSRNOG00060002173
resolver
ensembl
ENSRNOG00065006868
resolver
ensp
ENSRNOP00000024347
resolver
genesymbol
Atp2a2
resolver
uniprot
P11508
resolver
uniprot_entry
AT2A2_RAT
resolver
uniprot_sec
P11508
resolver
activity_regulation
ACTIVITY REGULATION: Has different conformational states with differential Ca2+ affinity. The E1 conformational state (active form) shows high Ca(2+) affinity, while the E2 state exhibits low Ca(2+) affinity. Binding of ATP allosterically increases its affinity for subsequent binding of Ca2+. Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. PLN inhibits ATP2A2 Ca(2+) affinity by disrupting its allosteric activation by ATP. Inhibited by sarcolipin (SLN) and myoregulin (MRLN). The inhibition is blocked by VMP1. Enhanced by STRIT1/DWORF; STRIT1 increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN). Stabilizes SERCA2 in its E2 state. {ECO:0000250|UniProtKB:O46674, ECO:0000250|UniProtKB:O55143, ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615, ECO:0000250|UniProtKB:Q8R429}.
uniprot
proteins
amino_acid_sequence
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFTITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEPGKECAQPATKPSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS
uniprot
proteins
ec_number
7.2.2.10
uniprot
proteins
function
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:O55143, ECO:0000250|UniProtKB:P16615}.; FUNCTION: [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation. {ECO:0000250|UniProtKB:O55143}.
uniprot
proteins
mass_dalton
114768
uniprot
proteins
post_translational_modification
PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IIA subfamily
uniprot
proteins
pubmed
10359649
uniprot
proteins
pubmed
16399855
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2542094
uniprot
proteins
pubmed
2844797
uniprot
proteins
sequence_length
1043
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|UniProtKB:O55143}.
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 757..776; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 787..807; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 828..850; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 897..916; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 930..948; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P04191"; TRANSMEM 964..984; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P04191
uniprot
proteins