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P04191

- AT2A1_RABIT

UniProt

P04191 - AT2A1_RABIT

Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

ATP2A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      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.

    Sites

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. calcium-transporting ATPase activity Source: UniProtKB
    4. 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. negative regulation of striated muscle contraction Source: UniProtKB
    5. positive regulation of fast-twitch skeletal muscle fiber contraction Source: UniProtKB
    6. regulation of striated muscle contraction Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP04191.

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    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. membrane Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. sarcoplasmic reticulum Source: BHF-UCL
    10. sarcoplasmic reticulum membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10011001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1PRO_0000046189Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP04191.

    Expressioni

    Tissue specificityi

    Skeletal muscle, fast twitch muscle (type II) fibers.1 Publication

    Developmental stagei

    Isoform SERCA1A and isoform SERCA1B are predominantly found in adult and neonatal skeletal muscle respectively.1 Publication

    Inductioni

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

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP04191. 5 interactions.

    Structurei

    Secondary structure

    1
    1001
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Helixi9 – 168
    Turni20 – 223
    Helixi26 – 3611
    Helixi49 – 546
    Helixi55 – 573
    Helixi60 – 7516
    Beta strandi76 – 783
    Beta strandi80 – 823
    Helixi83 – 853
    Beta strandi86 – 883
    Helixi89 – 11123
    Helixi115 – 1195
    Helixi120 – 1223
    Beta strandi125 – 1317
    Beta strandi138 – 1414
    Helixi142 – 1443
    Beta strandi150 – 1545
    Beta strandi161 – 1688
    Beta strandi170 – 1723
    Beta strandi173 – 1764
    Helixi178 – 1814
    Beta strandi187 – 1893
    Helixi201 – 2033
    Beta strandi213 – 2164
    Beta strandi218 – 2258
    Helixi227 – 2293
    Helixi231 – 24010
    Helixi248 – 27326
    Helixi274 – 2807
    Beta strandi283 – 2864
    Helixi288 – 30619
    Helixi311 – 32818
    Beta strandi331 – 3344
    Helixi338 – 3436
    Beta strandi347 – 3526
    Turni353 – 3553
    Beta strandi362 – 37312
    Beta strandi376 – 3849
    Beta strandi387 – 3915
    Beta strandi395 – 3973
    Beta strandi400 – 4023
    Helixi404 – 4063
    Helixi408 – 41912
    Beta strandi424 – 4285
    Turni429 – 4324
    Beta strandi433 – 4386
    Helixi440 – 45213
    Beta strandi460 – 4623
    Turni464 – 4663
    Helixi467 – 4693
    Helixi470 – 4789
    Beta strandi479 – 48810
    Turni489 – 4924
    Beta strandi493 – 50210
    Helixi503 – 5086
    Beta strandi511 – 5166
    Helixi518 – 5236
    Beta strandi525 – 5306
    Beta strandi533 – 5364
    Helixi539 – 55416
    Turni555 – 5573
    Beta strandi560 – 56910
    Helixi573 – 5753
    Helixi581 – 5833
    Helixi584 – 5874
    Beta strandi590 – 60011
    Helixi607 – 61610
    Beta strandi620 – 6278
    Helixi629 – 63810
    Beta strandi640 – 6423
    Turni649 – 6513
    Beta strandi652 – 6543
    Helixi655 – 6595
    Helixi663 – 67210
    Beta strandi675 – 6784
    Helixi683 – 69210
    Turni693 – 6953
    Beta strandi698 – 7025
    Helixi705 – 7073
    Helixi708 – 7136
    Beta strandi716 – 7205
    Helixi725 – 7295
    Beta strandi732 – 7354
    Helixi740 – 78041
    Helixi789 – 7979
    Turni798 – 8003
    Helixi801 – 8077
    Helixi816 – 8183
    Beta strandi824 – 8263
    Helixi831 – 85525
    Turni856 – 8583
    Beta strandi860 – 8623
    Turni866 – 8683
    Helixi870 – 8723
    Helixi873 – 8753
    Beta strandi876 – 8794
    Turni880 – 8823
    Beta strandi884 – 8863
    Helixi890 – 8923
    Helixi894 – 91320
    Beta strandi916 – 9194
    Turni922 – 9243
    Helixi927 – 9293
    Helixi931 – 94919
    Helixi952 – 9565
    Helixi964 – 97411
    Helixi976 – 99015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FQUmodel-A1-993[»]
    1IWOX-ray3.10A/B1-994[»]
    1KJUelectron microscopy6.00A1-994[»]
    1SU4X-ray2.40A1-994[»]
    1T5SX-ray2.60A1-993[»]
    1T5TX-ray2.90A1-993[»]
    1VFPX-ray2.90A/B1-994[»]
    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 microscopy18.00B36-77[»]
    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-ray2.50A1-994[»]
    3AR3X-ray2.30A1-994[»]
    3AR4X-ray2.15A1-994[»]
    3AR5X-ray2.20A1-994[»]
    3AR6X-ray2.20A1-994[»]
    3AR7X-ray2.15A1-994[»]
    3AR8X-ray2.60A1-994[»]
    3AR9X-ray2.60A1-994[»]
    3B9BX-ray2.65A1-993[»]
    3B9RX-ray3.00A/B1-993[»]
    3BA6X-ray2.80A1-993[»]
    3FGOX-ray2.50A/B1-994[»]
    3FPBX-ray2.55A1-994[»]
    3FPSX-ray3.20A1-994[»]
    3N5KX-ray2.20A/B1-994[»]
    3N8GX-ray2.58A1-993[»]
    3W5AX-ray3.01A/B1-993[»]
    3W5BX-ray3.20A1-993[»]
    3W5CX-ray2.50A1-993[»]
    3W5DX-ray2.45A1-993[»]
    4BEWX-ray2.50A/B1-994[»]
    4H1WX-ray3.10A1-993[»]
    4J2TX-ray3.20A1-993[»]
    4KYTX-ray2.83A1-993[»]
    4NABX-ray3.50A1-993[»]
    ProteinModelPortaliP04191.
    SMRiP04191. Positions 1-993.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04191.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicAdd
    BLAST
    Topological domaini70 – 8920LumenalAdd
    BLAST
    Topological domaini111 – 253143CytoplasmicAdd
    BLAST
    Topological domaini274 – 29522LumenalAdd
    BLAST
    Topological domaini314 – 757444CytoplasmicAdd
    BLAST
    Topological domaini778 – 78710Lumenal
    Topological domaini809 – 82820CytoplasmicAdd
    BLAST
    Topological domaini852 – 89746LumenalAdd
    BLAST
    Topological domaini918 – 93013CytoplasmicAdd
    BLAST
    Topological domaini950 – 96415LumenalAdd
    BLAST
    Topological domaini986 – 100116CytoplasmicAdd
    BLAST

    Transmembrane

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

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOVERGENiHBG105648.

    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. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform SERCA1B (identifier: P04191-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW     50
    ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA 100
    NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI 150
    VEVAVGDKVP ADIRILSIKS TTLRVDQSIL TGESVSVIKH TEPVPDPRAV 200
    NQDKKNMLFS GTNIAAGKAL GIVATTGVST EIGKIRDQMA ATEQDKTPLQ 250
    QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV 300
    ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
    DKTGTLTTNQ MSVCKMFIID KVDGDFCSLN EFSITGSTYA PEGEVLKNDK 400
    PIRSGQFDGL VELATICALC NDSSLDFNET KGVYEKVGEA TETALTTLVE 450
    KMNVFNTEVR NLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP 500
    AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPMTGP VKEKILSVIK 550
    EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML 600
    DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD 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
    AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA 900
    LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV 950
    DPLPMIFKLK ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR 1000
    K 1001
    Length:1,001
    Mass (Da):110,459
    Last modified:March 20, 1987 - v1
    Checksum:i1F0D8C36CF975266
    GO
    Isoform SERCA1A (identifier: P04191-2) [UniParc]FASTAAdd to Basket

    Also known as: Adult

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

    Show »
    Length:994
    Mass (Da):109,490
    Checksum:i148C462A8653A3E5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei994 – 10018DPEDERRK → G in isoform SERCA1A. 1 PublicationVSP_000356

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12898 mRNA. Translation: AAA31165.1.
    M15351 mRNA. Translation: AAA31166.1.
    M15158 mRNA. Translation: AAA31167.1.
    PIRiA01075. PWRBFC.
    RefSeqiNP_001082787.1. NM_001089318.1. [P04191-1]
    UniGeneiOcu.1829.
    Ocu.6937.

    Genome annotation databases

    GeneIDi100037716.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12898 mRNA. Translation: AAA31165.1 .
    M15351 mRNA. Translation: AAA31166.1 .
    M15158 mRNA. Translation: AAA31167.1 .
    PIRi A01075. PWRBFC.
    RefSeqi NP_001082787.1. NM_001089318.1. [P04191-1 ]
    UniGenei Ocu.1829.
    Ocu.6937.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FQU model - A 1-993 [» ]
    1IWO X-ray 3.10 A/B 1-994 [» ]
    1KJU electron microscopy 6.00 A 1-994 [» ]
    1SU4 X-ray 2.40 A 1-994 [» ]
    1T5S X-ray 2.60 A 1-993 [» ]
    1T5T X-ray 2.90 A 1-993 [» ]
    1VFP X-ray 2.90 A/B 1-994 [» ]
    1WPG X-ray 2.30 A/B/C/D 1-993 [» ]
    1XP5 X-ray 3.00 A 1-993 [» ]
    2AGV X-ray 2.40 A/B 1-993 [» ]
    2BY4 X-ray 3.30 A 1-993 [» ]
    2C88 X-ray 3.10 A 1-993 [» ]
    2C8K X-ray 2.80 A 1-993 [» ]
    2C8L X-ray 3.10 A 1-993 [» ]
    2C9M X-ray 3.00 A/B 1-993 [» ]
    2DQS X-ray 2.50 A 1-993 [» ]
    2EAR X-ray 3.10 A 1-993 [» ]
    2EAS X-ray 3.40 A 1-993 [» ]
    2EAT X-ray 2.90 A 1-993 [» ]
    2EAU X-ray 2.80 A 1-993 [» ]
    2O9J X-ray 2.65 A 1-993 [» ]
    2OA0 X-ray 3.40 A 1-993 [» ]
    2VOY electron microscopy 18.00 B 36-77 [» ]
    C 967-988 [» ]
    D 832-854 [» ]
    E 86-115 [» ]
    G 243-278 [» ]
    H 289-336 [» ]
    K 749-780 [» ]
    L 789-809 [» ]
    2YFY X-ray 3.10 A 1-993 [» ]
    2ZBD X-ray 2.40 A 1-993 [» ]
    2ZBE X-ray 3.80 A/B 1-993 [» ]
    2ZBF X-ray 2.40 A 1-993 [» ]
    2ZBG X-ray 2.55 A 1-993 [» ]
    3AR2 X-ray 2.50 A 1-994 [» ]
    3AR3 X-ray 2.30 A 1-994 [» ]
    3AR4 X-ray 2.15 A 1-994 [» ]
    3AR5 X-ray 2.20 A 1-994 [» ]
    3AR6 X-ray 2.20 A 1-994 [» ]
    3AR7 X-ray 2.15 A 1-994 [» ]
    3AR8 X-ray 2.60 A 1-994 [» ]
    3AR9 X-ray 2.60 A 1-994 [» ]
    3B9B X-ray 2.65 A 1-993 [» ]
    3B9R X-ray 3.00 A/B 1-993 [» ]
    3BA6 X-ray 2.80 A 1-993 [» ]
    3FGO X-ray 2.50 A/B 1-994 [» ]
    3FPB X-ray 2.55 A 1-994 [» ]
    3FPS X-ray 3.20 A 1-994 [» ]
    3N5K X-ray 2.20 A/B 1-994 [» ]
    3N8G X-ray 2.58 A 1-993 [» ]
    3W5A X-ray 3.01 A/B 1-993 [» ]
    3W5B X-ray 3.20 A 1-993 [» ]
    3W5C X-ray 2.50 A 1-993 [» ]
    3W5D X-ray 2.45 A 1-993 [» ]
    4BEW X-ray 2.50 A/B 1-994 [» ]
    4H1W X-ray 3.10 A 1-993 [» ]
    4J2T X-ray 3.20 A 1-993 [» ]
    4KYT X-ray 2.83 A 1-993 [» ]
    4NAB X-ray 3.50 A 1-993 [» ]
    ProteinModelPortali P04191.
    SMRi P04191. Positions 1-993.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04191. 5 interactions.

    Chemistry

    BindingDBi P04191.
    ChEMBLi CHEMBL4693.

    Proteomic databases

    PRIDEi P04191.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100037716.

    Organism-specific databases

    CTDi 487.

    Phylogenomic databases

    eggNOGi COG0474.
    HOVERGENi HBG105648.

    Enzyme and pathway databases

    SABIO-RK P04191.

    Miscellaneous databases

    EvolutionaryTracei P04191.

    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. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiAT2A1_RABIT
    AccessioniPrimary (citable) accession number: P04191
    Secondary accession number(s): P11719
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3