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Q64578

- AT2A1_RAT

UniProt

Q64578 - AT2A1_RAT

Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

Atp2a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi304 – 3041Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi305 – 3051Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi307 – 3071Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi309 – 3091Calcium 2By similarity
    Active sitei351 – 35114-aspartylphosphate intermediateBy similarity
    Metal bindingi703 – 7031MagnesiumBy similarity
    Metal bindingi707 – 7071MagnesiumBy similarity
    Metal bindingi768 – 7681Calcium 1By similarity
    Metal bindingi771 – 7711Calcium 1By similarity
    Metal bindingi796 – 7961Calcium 2By similarity
    Metal bindingi799 – 7991Calcium 1By similarity
    Metal bindingi800 – 8001Calcium 1By similarity
    Metal bindingi800 – 8001Calcium 2By similarity
    Metal bindingi908 – 9081Calcium 1By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. calcium-transporting ATPase activity Source: UniProtKB
    4. nucleotide-sugar transmembrane transporter activity Source: RGD
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: UniProtKB
    2. calcium ion transmembrane transport Source: GOC
    3. calcium ion transport Source: UniProtKB
    4. carbohydrate derivative transport Source: GOC
    5. negative regulation of striated muscle contraction Source: UniProtKB
    6. nucleotide transmembrane transport Source: GOC
    7. positive regulation of fast-twitch skeletal muscle fiber contraction Source: UniProtKB
    8. regulation of muscle contraction Source: RGD
    9. regulation of striated muscle contraction Source: UniProtKB
    10. response to peptide hormone Source: UniProtKB
    11. sarcoplasmic reticulum calcium ion transport Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (EC:3.6.3.8)
    Short name:
    SERCA1
    Short name:
    SR Ca(2+)-ATPase 1
    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 namesi
    Name:Atp2a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621293. Atp2a1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. H zone Source: UniProtKB
    5. I band Source: UniProtKB
    6. integral component of membrane Source: UniProtKB-KW
    7. intracellular membrane-bounded organelle Source: RGD
    8. membrane Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. sarcoplasmic reticulum Source: UniProtKB
    11. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 994994Sarcoplasmic/endoplasmic reticulum calcium ATPase 1PRO_0000046190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi876 ↔ 888By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ64578.

    PTM databases

    PhosphoSiteiQ64578.

    Expressioni

    Tissue specificityi

    Skeletal muscle, fast twitch muscle (type II) fibers.

    Inductioni

    Increased contractile activity leads to a decrease in SERCA1 expression, while decreased contractile activity leads to an increase in SERCA1 expression.

    Gene expression databases

    GenevestigatoriQ64578.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ64578.
    SMRiQ64578. Positions 1-994.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicBy similarityAdd
    BLAST
    Topological domaini70 – 8920LumenalBy similarityAdd
    BLAST
    Topological domaini111 – 253143CytoplasmicBy similarityAdd
    BLAST
    Topological domaini274 – 29522LumenalBy similarityAdd
    BLAST
    Topological domaini314 – 757444CytoplasmicBy similarityAdd
    BLAST
    Topological domaini778 – 78710LumenalBy similarity
    Topological domaini809 – 82820CytoplasmicBy similarityAdd
    BLAST
    Topological domaini852 – 89746LumenalBy similarityAdd
    BLAST
    Topological domaini918 – 93013CytoplasmicBy similarityAdd
    BLAST
    Topological domaini950 – 96415LumenalBy similarityAdd
    BLAST
    Topological domaini986 – 9949CytoplasmicBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921Helical; Name=1By similarityAdd
    BLAST
    Transmembranei90 – 11021Helical; Name=2By similarityAdd
    BLAST
    Transmembranei254 – 27320Helical; Name=3By similarityAdd
    BLAST
    Transmembranei296 – 31318Helical; Name=4By similarityAdd
    BLAST
    Transmembranei758 – 77720Helical; Name=5By similarityAdd
    BLAST
    Transmembranei788 – 80821Helical; Name=6By similarityAdd
    BLAST
    Transmembranei829 – 85123Helical; Name=7By similarityAdd
    BLAST
    Transmembranei898 – 91720Helical; Name=8By similarityAdd
    BLAST
    Transmembranei931 – 94919Helical; Name=9By similarityAdd
    BLAST
    Transmembranei965 – 98521Helical; Name=10By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 40031Interacts with phospholamban 1By similarityAdd
    BLAST
    Regioni788 – 80821Interacts with phospholamban 2By similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG105648.
    KOiK05853.
    PhylomeDBiQ64578.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR005782. 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]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q64578-1 [UniParc]FASTAAdd to Basket

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    MEAAHSKSTE ECLSYFGVSE TTGLTPDQVK RHLEKYGPNE LPAEEGKSLW    50
    ELVVEQFEDL LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA 100
    NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI 150
    VEVAVGDKVP ADIRILSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV 200
    NQDKKNMLFS GTNIAAGKAV GIVATTGVST EIGKIRDQMA ATEQDKTPLQ 250
    QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV 300
    ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
    DKTGTLTTNQ MSVCKMFIID KVDGDICSLN EFSITGSTYA PEGEVLKNDK 400
    PVRAGQYDGL VELATICALC NDSSLDFNET KGVYEKVGEA TETALTTLVE 450
    KMNVFNTEVR SLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP 500
    AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP VKEKIMSVIK 550
    EWGTGRDTLR CLALATRDTP PKREEMVLDD SAKFMEYEMD LTFVGVVGML 600
    DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFSENEEVAD 650
    RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM 700
    TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG 750
    RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD 800
    GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG 850
    AAAWWFLYAE DGPHVSYHQL THFMQCTEHN PEFDGLDCEV FEAPEPMTMA 900
    LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV 950
    DPLPMIFKLR ALDFTQWLMV LKISLPVIGL DELLKFIARN YLEG 994
    Length:994
    Mass (Da):109,409
    Last modified:November 1, 1996 - v1
    Checksum:i899F91AD8038A47A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99223 mRNA. Translation: AAA40991.1.
    AF091853 Genomic DNA. Translation: AAD17802.1.
    AF091852 Genomic DNA. Translation: AAD17801.1.
    PIRiA48849.
    RefSeqiNP_478120.1. NM_058213.1.
    UniGeneiRn.217139.

    Genome annotation databases

    GeneIDi116601.
    KEGGirno:116601.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99223 mRNA. Translation: AAA40991.1 .
    AF091853 Genomic DNA. Translation: AAD17802.1 .
    AF091852 Genomic DNA. Translation: AAD17801.1 .
    PIRi A48849.
    RefSeqi NP_478120.1. NM_058213.1.
    UniGenei Rn.217139.

    3D structure databases

    ProteinModelPortali Q64578.
    SMRi Q64578. Positions 1-994.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q64578.

    Proteomic databases

    PRIDEi Q64578.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116601.
    KEGGi rno:116601.

    Organism-specific databases

    CTDi 487.
    RGDi 621293. Atp2a1.

    Phylogenomic databases

    HOVERGENi HBG105648.
    KOi K05853.
    PhylomeDBi Q64578.

    Miscellaneous databases

    NextBioi 619311.
    PROi Q64578.

    Gene expression databases

    Genevestigatori Q64578.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi 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 ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-994.
      Strain: Sprague-Dawley.
      Tissue: Kidney.

    Entry informationi

    Entry nameiAT2A1_RAT
    AccessioniPrimary (citable) accession number: Q64578
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3