Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

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Q92105 (AT2A1_RANES) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rana esculenta (Edible frog) (Pelophylax esculentus)

Taxonomic identifier

8401 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Pelophylax

Protein attributes

Sequence length	994 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane Sarcoplasmic reticulum
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Gene Ontology (GO)
Biological_process	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
Cellular_component	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 endoplasmic reticulum-Golgi intermediate compartment Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW 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_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
Complete GO annotation...

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_0000046193

Regions

Topological domain

1 – 48

Cytoplasmic By similarity

Transmembrane

49 – 69

Helical; Name=1; By similarity

Topological domain

70 – 89

Lumenal By similarity

Transmembrane

90 – 110

Helical; Name=2; By similarity

Topological domain

111 – 253

143

Cytoplasmic By similarity

Transmembrane

254 – 273

Helical; Name=3; By similarity

Topological domain

274 – 295

Lumenal By similarity

Transmembrane

296 – 313

Helical; Name=4; By similarity

Topological domain

314 – 757

444

Cytoplasmic By similarity

Transmembrane

758 – 777

Helical; Name=5; By similarity

Topological domain

778 – 787

Lumenal By similarity

Transmembrane

788 – 808

Helical; Name=6; By similarity

Topological domain

809 – 828

Cytoplasmic By similarity

Transmembrane

829 – 851

Helical; Name=7; By similarity

Topological domain

852 – 897

Lumenal By similarity

Transmembrane

898 – 917

Helical; Name=8; By similarity

Topological domain

918 – 930

Cytoplasmic By similarity

Transmembrane

931 – 949

Helical; Name=9; By similarity

Topological domain

950 – 964

Lumenal By similarity

Transmembrane

965 – 985

Helical; Name=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

Sequences

Sequence

Length

Mass (Da)

Tools

Q92105 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 71ECBD003E4498A7
Show »

FASTA

994

109,288

        10         20         30         40         50         60 
MEQAHTKTTE ECLAYFGVNE NTGLSLDQVK KNFDKFGPNE LPAEEGKSLW ELVAEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAI ISFVLAWFEE GEETVTAFVE PFVILLILIA NAVVGVWQER NAEDAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RSDRKSVQRI KARELVPGDI VEVAVGDKVP ADIRLISIKS TTLRIDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TEVVPDTRAV NQDKKNMLFS GTNVGAGKAV GVVIATGPNT EIGKIRDEMA 

       250        260        270        280        290        300 
ATEQEKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPIHGGSWIK GAIYYFKIAV 

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

       370        380        390        400        410        420 
MSVCRMFVID KVEGDVTSLN EFTITGSTYA PEGDVQKNDK NVKAGQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSSLDFNES KGVFEKVGEA TETALTTLVE KMNVFNTDVK SLSKVERANA CNSVIKQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCIP AKASRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTSA 

       550        560        570        580        590        600 
IKDKILSVVK EWGTGRDTLR CLALATRDTP PKREDMVLDE ATRFIEYETD LTFVGCVGML 

       610        620        630        640        650        660 
DPPRKEVMGS IQLCREAGIR VIMITGDNKG TAIAICRRIG IFGEDDDVSG RAFTGREFDD 

       670        680        690        700        710        720 
LPPAEQREAC KRASCFARVE PAHKSKIVEF LQSFDEITAM 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 AAAWWFMYAD DGPNVTFYQL SHFMQCTEDN PDFEGHECEI FESPVPMTMA 

       910        920        930        940        950        960 
LSVLVTIEMC NALNSLSENQ SLIRMPPWSN FWLLGSICLS MSLHFLILYV EPLPMIFKLT 

       970        980        990 
PLNVEQWFIV LKMSFPVILL DELLKFVARN YLEG

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References

[1]

"Deduced amino acid sequence and E1-E2 equilibrium of the sarcoplasmic reticulum Ca(2+)-ATPase of frog skeletal muscle. Comparison with the Ca(2+)-ATPase of rabbit fast twitch muscle."
Vilsen B., Andersen J.P.
FEBS Lett. 306:213-218(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fast-twitch skeletal muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63009 mRNA. Translation: CAA44737.1.
PIR	S24359.
3D structure databases
ProteinModelPortal	Q92105.
SMR	Q92105. Positions 1-994.
ModBase	Search...
Proteomic databases
PRIDE	Q92105.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG105648.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR005782. 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]
PANTHER	PTHR24093. PTHR24093. 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]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AT2A1_RANES

Accession

Primary (citable) accession number: Q92105

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents