Q64518 · AT2A3_MOUSE
- ProteinSarcoplasmic/endoplasmic reticulum calcium ATPase 3
- GeneAtp2a3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids999 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Catalytic activity
- ATP + Ca2+(in) + H2O = ADP + Ca2+(out) + H+ + phosphateThis reaction proceeds in the forward direction.
CHEBI:30616 + Ca2+ (in)CHEBI:29108+ CHEBI:15377 = CHEBI:456216 + Ca2+ (out)CHEBI:29108+ CHEBI:15378 + CHEBI:43474
Cofactor
Activity regulation
Inhibited by sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).
Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).
Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 304 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 305 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 307 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 309 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 351 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 351 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 353 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 442 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 489 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 515 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 560 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 625 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 626 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 627 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 678 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 684 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 703 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 706 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 768 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 771 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 796 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 799 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 800 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 800 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 908 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | membrane | |
Cellular Component | sarcoplasmic reticulum membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | calcium ion transmembrane transporter activity | |
Molecular Function | calcium-dependent ATPase activity | |
Molecular Function | cysteine-type endopeptidase activator activity involved in apoptotic process | |
Molecular Function | metal ion binding | |
Molecular Function | P-type calcium transporter activity | |
Molecular Function | transmembrane transporter binding | |
Biological Process | calcium ion transmembrane transport | |
Biological Process | calcium ion transport from cytosol to endoplasmic reticulum | |
Biological Process | endoplasmic reticulum calcium ion homeostasis | |
Biological Process | intracellular calcium ion homeostasis | |
Biological Process | intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSarcoplasmic/endoplasmic reticulum calcium ATPase 3
- EC number
- Short namesSERCA3; SR Ca(2+)-ATPase 3
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64518
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Sarcoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-48 | Cytoplasmic | ||||
Sequence: MEEAHLLSAADVLRRFSVTAEGGLSLEQVTDARERYGPNELPTEEGKS | ||||||
Transmembrane | 49-69 | Helical; Name=1 | ||||
Sequence: LWELVVEQFEDLLVRILLLAA | ||||||
Topological domain | 70-89 | Lumenal | ||||
Sequence: LVSFVLAWFEEGEETTTAFV | ||||||
Transmembrane | 90-110 | Helical; Name=2 | ||||
Sequence: EPLVIMLILVANAIVGVWQER | ||||||
Topological domain | 111-253 | Cytoplasmic | ||||
Sequence: NAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSILTGESVSVTKHTDAIPDPRAVNQDKKNMLFSGTNIASGKALGVAVATGLQTELGKIRSQMAAVEPERTPLQRKL | ||||||
Transmembrane | 254-273 | Helical; Name=3 | ||||
Sequence: DEFGRQLSHAISVICVAVWV | ||||||
Topological domain | 274-295 | Lumenal | ||||
Sequence: INIGHFADPAHGGSWLRGAVYY | ||||||
Transmembrane | 296-313 | Helical; Name=4 | ||||
Sequence: FKIAVALAVAAIPEGLPA | ||||||
Topological domain | 314-757 | Cytoplasmic | ||||
Sequence: VITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEAEAGTCRLHEFTISGTTYTPEGEVRQGEQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLKGLSRVERAGACNSVIKQLMRKEFTLEFSRDRKSMSVYCTPTRADPKVQGSKMFVKGAPESVIERCSSVRVGSRTAPLSTTSREHILAKIRDWGSGSDTLRCLALATRDTPPRKEDMHLDDCSRFVQYETDLTFVGCVGMLDPPRPEVAACITRCSRAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVLGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYNNM | ||||||
Transmembrane | 758-777 | Helical; Name=5 | ||||
Sequence: KQFIRYLISSNVGEVVCIFL | ||||||
Topological domain | 778-787 | Lumenal | ||||
Sequence: TAILGLPEAL | ||||||
Transmembrane | 788-808 | Helical; Name=6 | ||||
Sequence: IPVQLLWVNLVTDGLPATALG | ||||||
Topological domain | 809-828 | Cytoplasmic | ||||
Sequence: FNPPDLDIMEKPPRNPREAL | ||||||
Transmembrane | 829-851 | Helical; Name=7 | ||||
Sequence: ISGWLFFRYLAIGVYVGLATVAA | ||||||
Topological domain | 852-897 | Lumenal | ||||
Sequence: ATWWFLYDTEGPQVTFYQLRNFLKCSEDNPLFAGIDCKVFESRFPT | ||||||
Transmembrane | 898-917 | Helical; Name=8 | ||||
Sequence: TMALSVLVTIEMCNALNSVS | ||||||
Topological domain | 918-930 | Cytoplasmic | ||||
Sequence: ENQSLLRMPPWLN | ||||||
Transmembrane | 931-949 | Helical; Name=9 | ||||
Sequence: PWLLGAVVMSMALHFLILL | ||||||
Topological domain | 950-964 | Lumenal | ||||
Sequence: VPPLPLIFQVTPLSG | ||||||
Transmembrane | 965-985 | Helical; Name=10 | ||||
Sequence: RQWGVVLQMSLPVILLDEALK | ||||||
Topological domain | 986-999 | Cytoplasmic | ||||
Sequence: YLSRNHMDEKKDLK |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 54 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000046203 | 1-999 | Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 | |||
Sequence: MEEAHLLSAADVLRRFSVTAEGGLSLEQVTDARERYGPNELPTEEGKSLWELVVEQFEDLLVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSILTGESVSVTKHTDAIPDPRAVNQDKKNMLFSGTNIASGKALGVAVATGLQTELGKIRSQMAAVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEAEAGTCRLHEFTISGTTYTPEGEVRQGEQPVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLKGLSRVERAGACNSVIKQLMRKEFTLEFSRDRKSMSVYCTPTRADPKVQGSKMFVKGAPESVIERCSSVRVGSRTAPLSTTSREHILAKIRDWGSGSDTLRCLALATRDTPPRKEDMHLDDCSRFVQYETDLTFVGCVGMLDPPRPEVAACITRCSRAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVLGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKPPRNPREALISGWLFFRYLAIGVYVGLATVAAATWWFLYDTEGPQVTFYQLRNFLKCSEDNPLFAGIDCKVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWLNPWLLGAVVMSMALHFLILLVPPLPLIFQVTPLSGRQWGVVLQMSLPVILLDEALKYLSRNHMDEKKDLK | ||||||
Modified residue | 17 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 19 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 25 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 415 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 662 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (By similarity).
Interacts with myoregulin (MRLN). Interacts with DWORF (By similarity).
Interacts with VMP1 (By similarity).
Interacts with TUNAR; the interaction occurs at low levels in low glucose conditions and is increased by high glucose levels (By similarity).
Interacts with phospholamban (PLN) (By similarity).
Interacts with myoregulin (MRLN). Interacts with DWORF (By similarity).
Interacts with VMP1 (By similarity).
Interacts with TUNAR; the interaction occurs at low levels in low glucose conditions and is increased by high glucose levels (By similarity).
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 370-400 | Interaction with phospholamban 1 | ||||
Sequence: AEAEAGTCRLHEFTISGTTYTPEGEVRQGEQ | ||||||
Region | 788-808 | Interaction with phospholamban 2 | ||||
Sequence: IPVQLLWVNLVTDGLPATALG |
Sequence similarities
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q64518-2
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameSERCA3A
- Length999
- Mass (Da)109,530
- Last updated2020-12-02 v4
- ChecksumF64B7046E792B6E7
Q64518-1
- NameSERCA3B
- Differences from canonical
- 994-999: EKKDLK → GVLGTFMQARSRQLPTTSRTPYHTGKKGPEVNPGSRGESPVWPSD
Q64518-3
- NameSERCA3C
- Differences from canonical
- 994-999: EKKDLK → GVLGTFMQARSRQLPTTSRTPYHTGLACKKKT
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 860 | in Ref. 1; AAB04098/AAB04099 | ||||
Sequence: T → A | ||||||
Alternative sequence | VSP_060850 | 994-999 | in isoform SERCA3B | |||
Sequence: EKKDLK → GVLGTFMQARSRQLPTTSRTPYHTGKKGPEVNPGSRGESPVWPSD | ||||||
Alternative sequence | VSP_060851 | 994-999 | in isoform SERCA3C | |||
Sequence: EKKDLK → GVLGTFMQARSRQLPTTSRTPYHTGLACKKKT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U49394 EMBL· GenBank· DDBJ | AAB04099.1 EMBL· GenBank· DDBJ | mRNA | ||
U49393 EMBL· GenBank· DDBJ | AAB04098.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466596 EMBL· GenBank· DDBJ | EDL12704.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC017639 EMBL· GenBank· DDBJ | AAH17639.1 EMBL· GenBank· DDBJ | mRNA | ||
Y15734 EMBL· GenBank· DDBJ | CAA75744.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15735 EMBL· GenBank· DDBJ | CAA75744.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15734 EMBL· GenBank· DDBJ | CAA75745.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15735 EMBL· GenBank· DDBJ | CAA75745.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15734 EMBL· GenBank· DDBJ | CAA75743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15735 EMBL· GenBank· DDBJ | CAA75743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y15736 EMBL· GenBank· DDBJ | CAA75746.1 EMBL· GenBank· DDBJ | Genomic DNA |