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Q0VCY0 (AT2A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length993 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 By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 993993Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
PRO_0000266030

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 – 9939Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 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

Disulfide bond875 ↔ 887 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VCY0 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: E6E3F70C527683C1

FASTA993109,290
        10         20         30         40         50         60 
MEAAHSKTTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVLEQFEDL 

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

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

       190        200        210        220        230        240 
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAI GIVATTGVGT EIGKIRDQMA 

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

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

       370        380        390        400        410        420 
MSVCKMFIID RIDGDLCLLN EFSVTGSTYA PEGEVLKNDK PVRSGQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSSLDFNET KGIYEKVGEA TETALTTLVE KMNVFNTEVR NLSKVERANA CNSVIRQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCSP AKSRAAVGNK MFVKGAPEGV IDRCNYVRVG TTRVPMTGPV 

       550        560        570        580        590        600 
KEKILSVIKE WGTGRDTLRC LALATRDTPP KREEMVLDDS TKFMEYETDL TFVGVVGMLD 

       610        620        630        640        650        660 
PPRKEVMGSI QLCRDAGIRV IMITGDNKGT AIAICRRIGI FGENEDVADR AYTGREFDDL 

       670        680        690        700        710        720 
PLAEQREACR RACCFARVEP THKSKIVEYL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG 

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

       790        800        810        820        830        840 
GLPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMDRPP RTPKEPLISG WLFFRYMAIG 

       850        860        870        880        890        900 
GYVGAATVGA AAWWFLYAED GPHVTYSQLT HFMKCSEHSP DFEGVDCEVF EAPQPMTMAL 

       910        920        930        940        950        960 
SVLVTIEMCN ALNSLSENQS LVRMPPWVNI WLVGSIGLSM SLHFLILYVD PLPMIFKLQA 

       970        980        990 
LDLYHWLMVL KISLPVIGLD EILKFVARNY LEG

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC119938 mRNA. Translation: AAI19939.1.
IPIIPI00711277.
RefSeqNP_001069235.1. NM_001075767.1.
UniGeneBt.62768.

3D structure databases

ProteinModelPortalQ0VCY0.
SMRQ0VCY0. Positions 1-993.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VCY0.

Proteomic databases

PRIDEQ0VCY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID518117.
KEGGbta:518117.

Organism-specific databases

CTD487.

Phylogenomic databases

eggNOGmaNOG17297.
GeneTreeENSGT00560000076887.
HOVERGENHBG105648.
PhylomeDBQ0VCY0.

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.
KOK05853.
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 nameAT2A1_BOVIN
AccessionPrimary (citable) accession number: Q0VCY0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 52 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

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