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P20647 (AT2A2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length1042 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 SERCA2A is involved in the regulation of the contraction/relaxation cycle.

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.

Subunit structure

Associated with phospholamban (PLN). Isoform SERCA2B interacts with TRAM2 (via C-terminus). Interacts with HAX1 By similarity.

Subcellular location

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

Tissue specificity

Isoform SERCA2A is highly expressed in heart and slow twitch skeletal muscle. Isoform SERCA2B 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]

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform SERCA2B (identifier: P20647-1)

Also known as: ATP2A2B;

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 SERCA2A (identifier: P20647-2)

Also known as: ATP2A2A;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPAPQSCSLWACTEGVSWPFVLLIVPLVMWVYSTDTNFSDLLWS → AILE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10421042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
PRO_0000046199

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 – 104258Cytoplasmic 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
Modified residue2951Nitrated tyrosine
Modified residue4641N6-acetyllysine By similarity
Modified residue5371Phosphothreonine By similarity
Modified residue6631Phosphoserine By similarity
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence994 – 104249GKECV…DLLWS → AILE in isoform SERCA2A.
VSP_000361

Experimental info

Sequence conflict5781K → E in AAA31150. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform SERCA2B (ATP2A2B) [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 4243836D67431575

FASTA1,042114,705
        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 KVDGDTCSLN EFTITGSTYA PIGEVHKDDK 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 STKVPMTAGV 

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

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

       670        680        690        700        710        720 
NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 

       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 
LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP APQSCSLWAC TEGVSWPFVL 

      1030       1040 
LIVPLVMWVY STDTNFSDLL WS

« Hide

Isoform SERCA2A (ATP2A2A) [UniParc].

Checksum: 1CE7B88F8A7BC12D
Show »

FASTA997109,644

References

[1]"Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic reticulum Ca2+-ATPase."
Lytton J., Zarain-Herzberg A., Periasamy M., McLennan D.H.
J. Biol. Chem. 264:7059-7065(1989) [PubMed: 2523389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2B).
Tissue: Smooth muscle.
[2]"Cloning of internal Ca pump from rabbit stomach smooth muscle."
Khan I., Grover A.K.
Nucleic Acids Res. 18:4026-4026(1990) [PubMed: 2165260] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2B).
Tissue: Smooth muscle.
[3]"Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence."
McLennan D.H., Brandl C.J., Korczak B., Green N.M.
Nature 316:696-700(1985) [PubMed: 2993904] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2A).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04703 mRNA. Translation: AAA31150.1.
X52496 mRNA. Translation: CAA36737.1.
X02814 mRNA. Translation: CAA26583.1.
PIRPWRBSC. A01076.
A33881.
PWRBMC. S10335.
RefSeqNP_001082790.1. NM_001089321.1.
UniGeneOcu.3251.

3D structure databases

ProteinModelPortalP20647.
SMRP20647. Positions 1-992.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100038308.

Organism-specific databases

CTD488.

Phylogenomic databases

HOVERGENHBG105648.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR005782. ATPase_P-typ_Ca-transp.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
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]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAT2A2_RABIT
AccessionPrimary (citable) accession number: P20647
Secondary accession number(s): P04192
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: July 15, 1999
Last modified: January 25, 2012
This is version 115 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents