Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

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P13585 (AT2A1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 112. 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

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro 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-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 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_0000046191

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

P13585 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 1F490D32F3EC319A
Show »

FASTA

994

109,023

        10         20         30         40         50         60 
MENAHAKTAE ECLAFFGVNE SVGLSGEQVR RALEKYGHNE LPAEEGKTIW ELVVEQFEDL 

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

       130        140        150        160        170        180 
EYEPEMGKVY RADRKAVQRI KARDLVPGDI AEVAVGDKVP ADIRIISIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIGAGKAV GIVVATGVNT EIGKIRDEMA 

       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 
MSVCKMFIVD KVEGDVCSLN EFSITGSTYA PEGDVLKNEK HIKAGQHDGL VELATICALC 

       430        440        450        460        470        480 
NDSSLDYNEA KGIYEKVGEA TETALTCLVE KMNVFNTDVR SLSKVERANA CNSVIKQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCSP AKASRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTPA 

       550        560        570        580        590        600 
VKEKILAVIK EWGTGRDTLR CLALATRDTP PKMEDMMLVD STKFAEYETD LTFVGCVGML 

       610        620        630        640        650        660 
DPPRKEVMGS IRLCRDAGIR VIMITGDNKG TAIAICRRIG IFTEDEEVSG RAYTGREFDD 

       670        680        690        700        710        720 
LPPAEQREAC RRACCFARVE PTHKSKIVEF LQSFDEITAM TGDGVNDAPA LKKAEIGIAM 

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

       790        800        810        820        830        840 
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDKP PRSPKEPLIS GWLFFRYLAI 

       850        860        870        880        890        900 
GGYVGAATVG AAAWWFLYAE DGPSLTYHQL THFMQCTHHN AEFEGVDCDI FESPVPMTMA 

       910        920        930        940        950        960 
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLVGSICLS MSLHFVILYV DPLPMIFKLT 

       970        980        990 
HLDLAHWLVV LRISFPVILL DEALKFVARN YLEA

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References

[1]	"Expression of avian Ca2+-ATPase in cultured mouse myogenic cells." Karin N.J., Kaprielian Z., Fambrough D.M. Mol. Cell. Biol. 9:1978-1986(1989) [PubMed: 2526293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Karin N.J. Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M26064 mRNA. Translation: AAA48609.1.
IPI	IPI00578635.
PIR	A32792.
RefSeq	NP_990850.1. NM_205519.1.
UniGene	Gga.877.
3D structure databases
ProteinModelPortal	P13585.
SMR	P13585. Positions 1-993.
ModBase	Search...
Proteomic databases
PRIDE	P13585.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396528.
KEGG	gga:396528.
Organism-specific databases
CTD	487.
Phylogenomic databases
HOVERGEN	HBG105648.
PhylomeDB	P13585.
Family and domain databases
InterPro	IPR023306. 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]
Gene3D	G3DSA: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.
KO	K05853.
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_CHICK

Accession

Primary (citable) accession number: P13585

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	May 1, 1991
Last modified:	January 25, 2012
This is version 112 of the entry and version 2 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents