Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q64578 (AT2A1_RAT)

Last modified February 9, 2010. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
      Short name=SR Ca(2+)-ATPase 1
      Short name=SERCA1
    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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length	994 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

Hide | Top

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⁺(Cis) = ADP + phosphate + Ca²⁺(Trans).
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 decrease SERCA1 expression, while decreased contractile activity leads to increase of SERCA1 expression.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro ATP catabolic process Inferred from sequence or structural similarity. Source: UniProtKB calcium ion transport Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of striated muscle contraction Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of fast-twitch skeletal muscle fiber contraction Inferred from sequence or structural similarity. Source: UniProtKB response to peptide hormone stimulus Inferred from direct assay. Source: UniProtKB
Cellular component	ER-Golgi intermediate compartment Inferred from sequence or structural similarity. Source: UniProtKB H zone Inferred from sequence or structural similarity. Source: UniProtKB I band Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: RGD perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB sarcoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP 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 magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide-sugar transmembrane transporter activity Inferred from direct assay. Source: RGD protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 994

994

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

PRO_0000046190

Regions

Topological domain

1 – 48

Cytoplasmic By similarity

Transmembrane

49 – 69

1 By similarity

Topological domain

70 – 89

Lumenal By similarity

Transmembrane

90 – 110

2 By similarity

Topological domain

111 – 253

143

Cytoplasmic By similarity

Transmembrane

254 – 273

3 By similarity

Topological domain

274 – 295

Lumenal By similarity

Transmembrane

296 – 313

4 By similarity

Topological domain

314 – 757

444

Cytoplasmic By similarity

Transmembrane

758 – 777

5 By similarity

Topological domain

778 – 787

Lumenal By similarity

Transmembrane

788 – 808

6 By similarity

Topological domain

809 – 828

Cytoplasmic By similarity

Transmembrane

829 – 851

7 By similarity

Topological domain

852 – 897

Lumenal By similarity

Transmembrane

898 – 917

8 By similarity

Topological domain

918 – 930

Cytoplasmic By similarity

Transmembrane

931 – 949

9 By similarity

Topological domain

950 – 964

Lumenal By similarity

Transmembrane

965 – 985

10 By similarity

Topological domain

986 – 994

Cytoplasmic By similarity

Region

370 – 400

Interacts with phospholamban 1 By similarity

Region

788 – 808

Interacts with phospholamban 2 By similarity

Sites

Active site

351

4-aspartylphosphate intermediate By similarity

Metal binding

304

Calcium 2; via carbonyl oxygen By similarity

Metal binding

305

Calcium 2; via carbonyl oxygen By similarity

Metal binding

307

Calcium 2; via carbonyl oxygen By similarity

Metal binding

309

Calcium 2 By similarity

Metal binding

703

Magnesium By similarity

Metal binding

707

Magnesium By similarity

Metal binding

768

Calcium 1 By similarity

Metal binding

771

Calcium 1 By similarity

Metal binding

796

Calcium 2 By similarity

Metal binding

799

Calcium 1 By similarity

Metal binding

800

Calcium 1 By similarity

Metal binding

800

Calcium 2 By similarity

Metal binding

908

Calcium 1 By similarity

Amino acid modifications

Disulfide bond

876 ↔ 888

By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q64578-1 [UniParc].

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

FASTA

994

109,409

        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

Hide | Top

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: 8447366] [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: 10329971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-994. Strain: Sprague-Dawley. Tissue: Kidney.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	M99223 mRNA. Translation: AAA40991.1. AF091853 Genomic DNA. Translation: AAD17802.1. AF091852 Genomic DNA. Translation: AAD17801.1.
IPI	IPI00213618.
PIR	A48849.
RefSeq	NP_478120.1.
UniGene	Rn.218029
3D structure databases
SMR	Q64578. Positions 1-994.
ModBase	Search...
Proteomic databases
PRIDE	Q64578.
Genome annotation databases
GeneID	116601.
KEGG	rno:116601.
Organism-specific databases
CTD	116601.
RGD	621293. Atp2a1.
Phylogenomic databases
HOVERGEN	Q64578.
PhylomeDB	Q64578.
Enzyme and pathway databases
BRENDA	3.6.3.8. 248.
Gene expression databases
Genevestigator	Q64578.
Family and domain databases
InterPro	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. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	619311.

Hide | Top

Entry information

Entry name

AT2A1_RAT

Accession

Primary (citable) accession number: Q64578

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents