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Q64578 (AT2A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Short name=SERCA1
Short name=SR Ca(2+)-ATPase 1
EC=3.6.3.8
Alternative name(s):
Calcium pump 1
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene names
Name:Atp2a1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length994 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Contributes to calcium sequestration involved in muscular excitation/contraction 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 sarcolipin (SLN) and phospholamban (PLN) By similarity.

Subcellular location

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

Tissue specificity

Skeletal muscle, fast twitch muscle (type II) fibers.

Induction

Increased contractile activity leads to a decrease in SERCA1 expression, while decreased contractile activity leads to an increase in SERCA1 expression.

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
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion transmembrane transport

Inferred from direct assay PubMed 12222829PubMed 12409282PubMed 9887021. Source: GOC

calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

carbohydrate derivative transport

Inferred from direct assay PubMed 12409282. Source: GOC

negative regulation of striated muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide transmembrane transport

Inferred from direct assay PubMed 12409282. Source: GOC

positive regulation of fast-twitch skeletal muscle fiber contraction

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of muscle contraction

Traceable author statement PubMed 12403631. Source: RGD

regulation of striated muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

response to peptide hormone

Inferred from direct assay PubMed 9295312. Source: UniProtKB

sarcoplasmic reticulum calcium ion transport

Inferred from direct assay PubMed 19029185. Source: RGD

   Cellular_componentH zone

Inferred from sequence or structural similarity. Source: UniProtKB

I band

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 14506614. Source: RGD

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-transporting ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide-sugar transmembrane transporter activity

Inferred from direct assay PubMed 12409282. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 994994Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
PRO_0000046190

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 – 757444Cytoplasmic By similarity
Transmembrane758 – 77720Helical; Name=5; By similarity
Topological domain778 – 78710Lumenal By similarity
Transmembrane788 – 80821Helical; Name=6; By similarity
Topological domain809 – 82820Cytoplasmic By similarity
Transmembrane829 – 85123Helical; Name=7; By similarity
Topological domain852 – 89746Lumenal By similarity
Transmembrane898 – 91720Helical; Name=8; By similarity
Topological domain918 – 93013Cytoplasmic By similarity
Transmembrane931 – 94919Helical; Name=9; By similarity
Topological domain950 – 96415Lumenal By similarity
Transmembrane965 – 98521Helical; Name=10; By similarity
Topological domain986 – 9949Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 By similarity
Region788 – 80821Interacts 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 binding7031Magnesium By similarity
Metal binding7071Magnesium By similarity
Metal binding7681Calcium 1 By similarity
Metal binding7711Calcium 1 By similarity
Metal binding7961Calcium 2 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding8001Calcium 1 By similarity
Metal binding8001Calcium 2 By similarity
Metal binding9081Calcium 1 By similarity

Amino acid modifications

Disulfide bond876 ↔ 888 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64578 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 899F91AD8038A47A

FASTA994109,409
        10         20         30         40         50         60 
MEAAHSKSTE ECLSYFGVSE TTGLTPDQVK RHLEKYGPNE LPAEEGKSLW ELVVEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAIVGVWQER NAENAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAV GIVATTGVST EIGKIRDQMA 

       250        260        270        280        290        300 
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV 

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

       370        380        390        400        410        420 
MSVCKMFIID KVDGDICSLN EFSITGSTYA PEGEVLKNDK PVRAGQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR SLSKVERANA CNSVIRQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP 

       550        560        570        580        590        600 
VKEKIMSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SAKFMEYEMD LTFVGVVGML 

       610        620        630        640        650        660 
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFSENEEVAD RAYTGREFDD 

       670        680        690        700        710        720 
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM 

       730        740        750        760        770        780 
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA 

       790        800        810        820        830        840 
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI 

       850        860        870        880        890        900 
GGYVGAATVG AAAWWFLYAE DGPHVSYHQL THFMQCTEHN PEFDGLDCEV FEAPEPMTMA 

       910        920        930        940        950        960 
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLR 

       970        980        990 
ALDFTQWLMV LKISLPVIGL DELLKFIARN YLEG 

« Hide

References

[1]"Molecular cloning and quantification of sarcoplasmic reticulum Ca(2+)-ATPase isoforms in rat muscles."
Wu K.D., Lytton J.
Am. J. Physiol. 264:C333-C341(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD Charles River.
Tissue: Skeletal muscle.
[2]"Unloading induces transcriptional activation of the sarco(endo)plasmic reticulum Ca2+-ATPase 1 gene in muscle."
Peters D.G., Mitchell-Felton H., Kandarian S.C.
Am. J. Physiol. 276:C1218-C1225(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-994.
Strain: Sprague-Dawley.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M99223 mRNA. Translation: AAA40991.1.
AF091853 Genomic DNA. Translation: AAD17802.1.
AF091852 Genomic DNA. Translation: AAD17801.1.
PIRA48849.
RefSeqNP_478120.1. NM_058213.1.
UniGeneRn.217139.

3D structure databases

ProteinModelPortalQ64578.
SMRQ64578. Positions 1-994.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ64578.

Proteomic databases

PRIDEQ64578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116601.
KEGGrno:116601.

Organism-specific databases

CTD487.
RGD621293. Atp2a1.

Phylogenomic databases

HOVERGENHBG105648.
KOK05853.
PhylomeDBQ64578.

Gene expression databases

GenevestigatorQ64578.

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. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619311.
PROQ64578.

Entry information

Entry nameAT2A1_RAT
AccessionPrimary (citable) accession number: Q64578
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 129 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