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P11507 (AT2A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Short name=SERCA2
Short name=SR Ca(2+)-ATPase 2
EC=3.6.3.8
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene names
Name:Atp2a2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1043 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2Ais involved in the regulation of the contraction/relaxation cycle By similarity.

Catalytic activity

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Enzyme regulation

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.

Subunit structure

Associated with phospholamban (PLN) By similarity. Isoform SERCA2Binteracts with TRAM2 (via C-terminus). Interacts with HAX1 By similarity. Interacts with S100A8 and S100A9 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Isoform 2 is highly expressed in heart and slow twitch skeletal muscle. Isoform 1 is widely expressed.

Post-translational modification

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity By similarity.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMIsopeptide bond
Nitration
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 21300842. Source: RGD

calcium ion transmembrane transport

Inferred from direct assay PubMed 12409282PubMed 21300842. Source: GOC

calcium ion transport

Inferred from direct assay PubMed 11595740. Source: RGD

regulation of muscle contraction

Traceable author statement PubMed 11595740. Source: RGD

response to peptide hormone

Inferred from direct assay PubMed 9295312PubMed 9295312. Source: UniProtKB

sarcoplasmic reticulum calcium ion transport

Inferred from direct assay PubMed 21300842. Source: RGD

   Cellular_componentextrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20177054. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20177054. Source: RGD

protein complex

Inferred from direct assay PubMed 17901878. Source: RGD

sarcoplasmic reticulum

Inferred from direct assay PubMed 12409282PubMed 17901878PubMed 8447366. Source: RGD

sarcoplasmic reticulum membrane

Inferred by curator PubMed 21300842. Source: RGD

vesicle membrane

Inferred from direct assay PubMed 21300842. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 12409282. Source: RGD

calcium ion binding

Inferred from direct assay PubMed 12409282. Source: RGD

calcium-transporting ATPase activity

Inferred from direct assay PubMed 12409282PubMed 21300842. Source: RGD

lutropin-choriogonadotropic hormone receptor binding

Inferred from physical interaction PubMed 17588601. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11507-1)

Also known as: Atp2a2b; SERCA2b;

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.
Isoform 2 (identifier: P11507-2)

Also known as: Atp2a2a; SERCA2a;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1043: GKECAQPATKPSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS → AILE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10431043Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
PRO_0000046200

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 6921Helical; Name=1; By similarity
Topological domain70 – 8920Lumenal By similarity
Transmembrane90 – 11021Helical; Name=2; By similarity
Topological domain111 – 253143Cytoplasmic By similarity
Transmembrane254 – 27320Helical; Name=3; By similarity
Topological domain274 – 29522Lumenal By similarity
Transmembrane296 – 31318Helical; Name=4; By similarity
Topological domain314 – 756443Cytoplasmic By similarity
Transmembrane757 – 77620Helical; Name=5; By similarity
Topological domain777 – 78610Lumenal By similarity
Transmembrane787 – 80721Helical; Name=6; By similarity
Topological domain808 – 82720Cytoplasmic By similarity
Transmembrane828 – 85023Helical; Name=7; By similarity
Topological domain851 – 89646Lumenal By similarity
Transmembrane897 – 91620Helical; Name=8; By similarity
Topological domain917 – 92913Cytoplasmic By similarity
Transmembrane930 – 94819Helical; Name=9; By similarity
Topological domain949 – 96315Lumenal By similarity
Transmembrane964 – 98421Helical; Name=10; By similarity
Topological domain985 – 104359Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 By similarity
Region575 – 59420Interacts with HAX1 By similarity
Region787 – 80721Interacts with phospholamban 2 By similarity

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2; via carbonyl oxygen By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3091Calcium 2 By similarity
Metal binding7021Magnesium By similarity
Metal binding7061Magnesium By similarity
Metal binding7671Calcium 1 By similarity
Metal binding7701Calcium 1 By similarity
Metal binding7951Calcium 2 By similarity
Metal binding7981Calcium 1 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding7991Calcium 2 By similarity
Metal binding9071Calcium 1 By similarity

Amino acid modifications

Modified residue2941Nitrated tyrosine Ref.4
Modified residue2951Nitrated tyrosine Ref.4
Modified residue6631Phosphoserine By similarity
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence994 – 104350GKECA…DMFWS → AILE in isoform 2.
VSP_000362

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Atp2a2b) (SERCA2b) [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 4B0B476BFD97F390

FASTA1,043114,768
        10         20         30         40         50         60 
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV 

       250        260        270        280        290        300 
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV 

       310        320        330        340        350        360 
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 

       370        380        390        400        410        420 
MSVCRMFILD KVEGDTCSLN EFTITGSTYA PIGEVQKDDK PVKCHQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV 

       550        560        570        580        590        600 
KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD 

       610        620        630        640        650        660 
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL 

       670        680        690        700        710        720 
SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG 

       730        740        750        760        770        780 
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL 

       790        800        810        820        830        840 
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG 

       850        860        870        880        890        900 
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL 

       910        920        930        940        950        960 
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP 

       970        980        990       1000       1010       1020 
LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECAQP ATKPSCSLSA CTDGISWPFV 

      1030       1040 
LLIMPLVVWV YSTDTNFSDM FWS 

« Hide

Isoform 2 (Atp2a2a) (SERCA2a) [UniParc].

Checksum: 3A14A6B604E97002
Show »

FASTA997109,681

References

[1]"A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site."
Gunteski-Hamblin A.-M., Greeb J., Shull G.E.
J. Biol. Chem. 263:15032-15040(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[2]"Characterization and expression of the rat heart sarcoplasmic reticulum Ca2+-ATPase mRNA."
Lompre A.M., de la Bastie D., Boheler K.R., Schwartz K.
FEBS Lett. 249:35-41(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart.
[3]"Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle."
Viner R.I., Ferrington D.A., Williams T.D., Bigelow D.J., Schoeneich C.
Biochem. J. 340:657-669(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION.
[4]"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-294 AND TYR-295.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04022 mRNA. Translation: AAA40785.1.
J04024 mRNA. Translation: AAA40787.1.
J04023 mRNA. Translation: AAA40786.1.
X15635 mRNA. Translation: CAA33645.1.
PIRA31982.
B31982.
RefSeqNP_001103609.1. NM_001110139.2.
NP_001104293.1. NM_001110823.2.
UniGeneRn.2305.

3D structure databases

ProteinModelPortalP11507.
SMRP11507. Positions 1-992.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248313. 1 interaction.
IntActP11507. 2 interactions.
MINTMINT-4563897.

PTM databases

PhosphoSiteP11507.

Proteomic databases

PaxDbP11507.
PRIDEP11507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29693.
KEGGrno:29693.
UCSCRGD:2174. rat. [P11507-1]

Organism-specific databases

CTD488.
RGD2174. Atp2a2.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265621.
HOVERGENHBG105648.
InParanoidP11507.
KOK05853.
PhylomeDBP11507.

Gene expression databases

GenevestigatorP11507.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR005782. ATPase_P-typ_Ca-transp_IIA.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610084.
PROP11507.

Entry information

Entry nameAT2A2_RAT
AccessionPrimary (citable) accession number: P11507
Secondary accession number(s): P11508
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families