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P04191 (AT2A1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length1001 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. 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.

Subunit structure

Associated with sarcolipin (SLN) By similarity and phospholamban (PLN).

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. Ref.6

Developmental stage

Isoform SERCA1A and isoform SERCA1B are predominantly found in adult and neonatal skeletal muscle respectively. Ref.6

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
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative 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

   Cellular_componentH 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

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 12585965. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12585965. Source: UniProtKB

sarcoplasmic reticulum

Inferred from direct assay PubMed 11438520PubMed 9575189. Source: UniProtKB

sarcoplasmic reticulum membrane

Traceable author statement PubMed 2993904. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from direct assay PubMed 11438520. Source: UniProtKB

calcium ion binding

Inferred from direct assay PubMed 11438520PubMed 16452481PubMed 9575189. Source: UniProtKB

calcium-transporting ATPase activity

Inferred from direct assay PubMed 10914677PubMed 11438520. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform SERCA1B (identifier: P04191-1)

Also known as: Neonatal;

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 SERCA1A (identifier: P04191-2)

Also known as: Adult;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1001: DPEDERRK → G

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10011001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
PRO_0000046189

Regions

Topological domain1 – 4848Cytoplasmic
Transmembrane49 – 6921Helical; Name=1
Topological domain70 – 8920Lumenal
Transmembrane90 – 11021Helical; Name=2
Topological domain111 – 253143Cytoplasmic
Transmembrane254 – 27320Helical; Name=3
Topological domain274 – 29522Lumenal
Transmembrane296 – 31318Helical; Name=4
Topological domain314 – 757444Cytoplasmic
Transmembrane758 – 77720Helical; Name=5
Topological domain778 – 78710Lumenal
Transmembrane788 – 80821Helical; Name=6
Topological domain809 – 82820Cytoplasmic
Transmembrane829 – 85123Helical; Name=7
Topological domain852 – 89746Lumenal
Transmembrane898 – 91720Helical; Name=8
Topological domain918 – 93013Cytoplasmic
Transmembrane931 – 94919Helical; Name=9
Topological domain950 – 96415Lumenal
Transmembrane965 – 98521Helical; Name=10
Topological domain986 – 100116Cytoplasmic
Region370 – 40031Interacts with phospholamban 1
Region788 – 80821Interacts with phospholamban 2

Sites

Active site35114-aspartylphosphate intermediate
Metal binding3041Calcium 2; via carbonyl oxygen
Metal binding3051Calcium 2; via carbonyl oxygen
Metal binding3071Calcium 2; via carbonyl oxygen
Metal binding3091Calcium 2
Metal binding7031Magnesium By similarity
Metal binding7071Magnesium By similarity
Metal binding7681Calcium 1
Metal binding7711Calcium 1
Metal binding7961Calcium 2
Metal binding7991Calcium 1
Metal binding8001Calcium 1
Metal binding8001Calcium 2
Metal binding9081Calcium 1

Amino acid modifications

Disulfide bond876 ↔ 888

Natural variations

Alternative sequence994 – 10018DPEDERRK → G in isoform SERCA1A.
VSP_000356

Secondary structure

1 ......................................................................................................................................................................................... 1001
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform SERCA1B (Neonatal) [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 1F0D8C36CF975266

FASTA1,001110,459
        10         20         30         40         50         60 
MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVIEQFEDL 

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

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

       190        200        210        220        230        240 
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVST 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 KVDGDFCSLN EFSITGSTYA PEGEVLKNDK PIRSGQFDGL VELATICALC 

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

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

       550        560        570        580        590        600 
VKEKILSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML 

       610        620        630        640        650        660 
DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD 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 AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA 

       910        920        930        940        950        960 
LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLK 

       970        980        990       1000 
ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR K

« Hide

Isoform SERCA1A (Adult) [UniParc].

Checksum: 148C462A8653A3E5
Show »

FASTA994109,490

References

[1]"Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences."
Brandl C.J., Green N.M., Korczak B., McLennan D.H.
Cell 44:597-607(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA1B).
[2]"Involvement of an arginyl residue in the nucleotide-binding site of Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal."
Corbalan-Garcia S., Teruel J.A., Gomez-Fernandez J.C.
Biochem. J. 318:179-185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 134-140 AND 490-495.
[3]"Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling."
Andersen J.P., Vilsen B., Collins J.H., Jorgensen P.L.
J. Membr. Biol. 93:85-92(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 199-212; 335-348 AND 506-519.
[4]"Chemical modification of the Ca(2+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum: identification of sites labeled with aryl isothiocyanates and thiol-directed conformational probes."
Wawrzynow A., Collins J.H.
Biochim. Biophys. Acta 1203:60-70(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 335-365; 468-476; 493-502; 513-529; 606-615; 630-637 AND 668-671.
[5]"Interaction of 4-azido-2-nitrophenyl phosphate, a pseudosubstrate, with the sarcoplasmic reticulum Ca-ATPase."
Lacapere J.J., Garin J.
Biochemistry 33:2586-2593(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 506-513 AND 584-591.
[6]"Adult forms of the Ca2+ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle."
Brandl C.J., Deleon S., Martin D.R., McLennan D.H.
J. Biol. Chem. 262:3768-3774(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1001 (ISOFORMS SERCA1A AND SERCA1B), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution."
Toyoshima C., Nakasako M., Nomura H., Ogawa H.
Nature 405:647-655(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ISOFORM SERCA1A.
[8]"Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban."
Toyofuku T., Kurzydlowski K., Tada M., McLennan D.H.
J. Biol. Chem. 268:2809-2815(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHOSPHOLAMBAN.
[9]"Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites."
Asahi M., Kimura Y., Kurzydlowski K., Tada M., McLennan D.H.
J. Biol. Chem. 274:32855-32862(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHOSPHOLAMBAN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12898 mRNA. Translation: AAA31165.1.
M15351 mRNA. Translation: AAA31166.1.
M15158 mRNA. Translation: AAA31167.1.
PIRPWRBFC. A01075.
RefSeqNP_001082787.1. NM_001089318.1.
UniGeneOcu.1829.
Ocu.6937.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQUmodel-A1-993[»]
1IWOX-ray3.10A/B1-993[»]
1KJUelectron microscopy6.00A1-993[»]
1SU4X-ray2.40A1-993[»]
1T5SX-ray2.60A1-993[»]
1T5TX-ray2.90A1-993[»]
1VFPX-ray2.90A/B1-993[»]
1WPGX-ray2.30A/B/C/D1-993[»]
1XP5X-ray3.00A1-993[»]
2AGVX-ray2.40A/B1-993[»]
2BY4X-ray3.30A1-993[»]
2C88X-ray3.10A1-993[»]
2C8KX-ray2.80A1-993[»]
2C8LX-ray3.10A1-993[»]
2C9MX-ray3.00A/B1-993[»]
2DQSX-ray2.50A1-993[»]
2EARX-ray3.10A1-993[»]
2EASX-ray3.40A1-993[»]
2EATX-ray2.90A1-993[»]
2EAUX-ray2.80A1-993[»]
2O9JX-ray2.65A1-993[»]
2OA0X-ray3.40A1-993[»]
2VOYelectron microscopy-B36-77[»]
C967-988[»]
D832-854[»]
E86-115[»]
G243-278[»]
H289-336[»]
K749-780[»]
L789-809[»]
2YFYX-ray3.10A1-993[»]
2ZBDX-ray2.40A1-993[»]
2ZBEX-ray3.80A/B1-993[»]
2ZBFX-ray2.40A1-993[»]
2ZBGX-ray2.55A1-993[»]
3AR2X-ray2.50A1-993[»]
3AR3X-ray2.30A1-993[»]
3AR4X-ray2.15A1-993[»]
3AR5X-ray2.20A1-993[»]
3AR6X-ray2.20A1-993[»]
3AR7X-ray2.15A1-993[»]
3AR8X-ray2.60A1-993[»]
3AR9X-ray2.60A1-993[»]
3B9BX-ray2.65A1-993[»]
3B9RX-ray3.00A/B1-993[»]
3BA6X-ray2.80A1-993[»]
3FGOX-ray2.50A/B1-993[»]
3FPBX-ray2.55A1-993[»]
3FPSX-ray3.20A1-993[»]
3N5KX-ray2.20A/B1-993[»]
3N8GX-ray2.58A1-993[»]
ProteinModelPortalP04191.
SMRP04191. Positions 1-993.
ModBaseSearch...

Protein-protein interaction databases

IntActP04191. 1 interaction.

Proteomic databases

PRIDEP04191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000027641; ENSOCUP00000018837; ENSOCUG00000002688.
GeneID100037716.

Organism-specific databases

CTD487.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076887.
HOVERGENHBG105648.

Enzyme and pathway databases

SABIO-RKP04191.

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]
PANTHERPTHR24093. PTHR24093. 1 hit.
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...

Other

BindingDBP04191.
ChEMBLCHEMBL4693.
EvolutionaryTraceP04191.

Entry information

Entry nameAT2A1_RABIT
AccessionPrimary (citable) accession number: P04191
Secondary accession number(s): P11719
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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