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P22700

- ATC1_DROME

UniProt

P22700 - ATC1_DROME

Protein

Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type

Gene

Ca-P60A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.

    Catalytic activityi

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

    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-KW
    2. calcium-transporting ATPase activity Source: FlyBase
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: FlyBase

    GO - Biological processi

    1. calcium ion transmembrane transport Source: GOC
    2. cellular calcium ion homeostasis Source: FlyBase
    3. flight behavior Source: FlyBase
    4. heart contraction Source: FlyBase
    5. intestinal stem cell homeostasis Source: FlyBase
    6. neuromuscular synaptic transmission Source: FlyBase
    7. positive regulation of calcium-transporting ATPase activity Source: FlyBase
    8. regulation of sequestering of calcium ion Source: FlyBase
    9. stabilization of membrane potential Source: FlyBase
    10. stem cell differentiation Source: FlyBase

    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:
    Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type (EC:3.6.3.8)
    Alternative name(s):
    Calcium ATPase at 60A
    Calcium pump
    Gene namesi
    Name:Ca-P60A
    ORF Names:CG3725
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0263006. Ca-P60A.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Sarcoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Colocalizes with SclA and SclB at the sarcoplasmic reticulum (SR) and the dyad, a structure in which the SR membrane lies closest to both the plasma membrane and the sarcomeres.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. lipid particle Source: FlyBase
    4. nuclear envelope Source: FlyBase
    5. sarcoplasmic reticulum Source: UniProtKB
    6. 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 – 10201020Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum typePRO_0000046208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei240 – 2401Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP22700.
    PRIDEiP22700.

    Expressioni

    Gene expression databases

    BgeeiP22700.

    Interactioni

    Subunit structurei

    Interacts with SclA and SclB.1 Publication

    Protein-protein interaction databases

    BioGridi72161. 103 interactions.
    DIPiDIP-20129N.
    IntActiP22700. 2 interactions.
    MINTiMINT-1567799.

    Structurei

    3D structure databases

    ProteinModelPortaliP22700.
    SMRiP22700. Positions 1-989.
    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 – 102035CytoplasmicBy similarityAdd
    BLAST

    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

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    GeneTreeiENSGT00560000076887.
    InParanoidiP22700.
    OMAiPKMEDMI.
    OrthoDBiEOG73Z2SF.
    PhylomeDBiP22700.

    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.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P22700-1) [UniParc]FASTAAdd to Basket

    Also known as: C, D, E, F, G, H

    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

    MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW     50
    QLVLEQFDDL LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA 100
    NAVVGVWQER NAESAIEALK EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL 150
    VEVSVGDKIP ADIRITHIYS TTLRIDQSIL TGESVSVIKH TDAIPDPRAV 200
    NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS ETEEIKTPLQ 250
    QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV 300
    ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
    DKTGTLTTNQ MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ 400
    RIKAADYDTL QELSTICIMC NDSAIDYNEF KQAFEKVGEA TETALIVLAE 450
    KLNSFSVNKS GLDRRSAAIA CRGEIETKWK KEFTLEFSRD RKSMSSYCTP 500
    LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA LKAKILALTG 550
    QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML 600
    DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG 650
    KSYSGREFDD LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM 700
    TGDGVNDAPA LKKAEIGIAM GSGTAVAKSA AEMVLADDNF SSIVSAVEEG 750
    RAIYNNMKQF IRYLISSNIG EVVSIFLTAA LGLPEALIPV QLLWVNLVTD 800
    GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI GFYVGAATVG 850
    AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA 900
    LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV 950
    DVLSTVFQVT PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK 1000
    MHGIVLMWAV FFGLLYAMML 1020

    Note: No experimental confirmation available.

    Length:1,020
    Mass (Da):111,701
    Last modified:December 1, 2000 - v2
    Checksum:i6A62D350BF316984
    GO
    Isoform A (identifier: P22700-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         994-1020: GESPIYKMHGIVLMWAVFFGLLYAMML → VPDVVVDRM

    Show »
    Length:1,002
    Mass (Da):109,611
    Checksum:i463400C1967BD7D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581K → R in AAL13694. (PubMed:12537569)Curated
    Sequence conflicti302 – 3021L → V in AAB00735. (PubMed:2148477)Curated
    Sequence conflicti357 – 3571T → L in CAA35505. (PubMed:2557235)Curated
    Sequence conflicti495 – 4951S → P in AAL13694. (PubMed:12537569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei994 – 102027GESPI…YAMML → VPDVVVDRM in isoform A. 1 PublicationVSP_010297Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62892 mRNA. Translation: AAB00735.1.
    AE013599 Genomic DNA. Translation: AAF47101.1.
    AE013599 Genomic DNA. Translation: AAF47102.1.
    AE013599 Genomic DNA. Translation: AAF47103.1.
    AE013599 Genomic DNA. Translation: AAM68278.1.
    AE013599 Genomic DNA. Translation: AAM68279.1.
    AE013599 Genomic DNA. Translation: AAM68280.1.
    AE013599 Genomic DNA. Translation: AAM68281.1.
    AY058465 mRNA. Translation: AAL13694.1.
    X17472 mRNA. Translation: CAA35505.1.
    PIRiA36691.
    RefSeqiNP_476832.1. NM_057484.2. [P22700-2]
    NP_726381.1. NM_166633.1. [P22700-1]
    NP_726382.1. NM_166634.1. [P22700-1]
    NP_726383.1. NM_166635.1. [P22700-1]
    NP_726384.1. NM_166636.1. [P22700-1]
    NP_726385.1. NM_166637.1. [P22700-1]
    NP_726386.1. NM_166638.1. [P22700-1]
    NP_726387.1. NM_166639.1. [P22700-1]
    UniGeneiDm.3812.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072211; FBpp0072120; FBgn0263006. [P22700-1]
    FBtr0072212; FBpp0072121; FBgn0263006. [P22700-1]
    FBtr0072213; FBpp0072122; FBgn0263006. [P22700-1]
    FBtr0072214; FBpp0072123; FBgn0263006. [P22700-1]
    FBtr0072216; FBpp0072125; FBgn0263006. [P22700-1]
    FBtr0072217; FBpp0072126; FBgn0263006. [P22700-1]
    FBtr0072218; FBpp0072127; FBgn0263006. [P22700-1]
    GeneIDi49297.
    KEGGidme:Dmel_CG3725.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62892 mRNA. Translation: AAB00735.1 .
    AE013599 Genomic DNA. Translation: AAF47101.1 .
    AE013599 Genomic DNA. Translation: AAF47102.1 .
    AE013599 Genomic DNA. Translation: AAF47103.1 .
    AE013599 Genomic DNA. Translation: AAM68278.1 .
    AE013599 Genomic DNA. Translation: AAM68279.1 .
    AE013599 Genomic DNA. Translation: AAM68280.1 .
    AE013599 Genomic DNA. Translation: AAM68281.1 .
    AY058465 mRNA. Translation: AAL13694.1 .
    X17472 mRNA. Translation: CAA35505.1 .
    PIRi A36691.
    RefSeqi NP_476832.1. NM_057484.2. [P22700-2 ]
    NP_726381.1. NM_166633.1. [P22700-1 ]
    NP_726382.1. NM_166634.1. [P22700-1 ]
    NP_726383.1. NM_166635.1. [P22700-1 ]
    NP_726384.1. NM_166636.1. [P22700-1 ]
    NP_726385.1. NM_166637.1. [P22700-1 ]
    NP_726386.1. NM_166638.1. [P22700-1 ]
    NP_726387.1. NM_166639.1. [P22700-1 ]
    UniGenei Dm.3812.

    3D structure databases

    ProteinModelPortali P22700.
    SMRi P22700. Positions 1-989.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 72161. 103 interactions.
    DIPi DIP-20129N.
    IntActi P22700. 2 interactions.
    MINTi MINT-1567799.

    Proteomic databases

    PaxDbi P22700.
    PRIDEi P22700.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072211 ; FBpp0072120 ; FBgn0263006 . [P22700-1 ]
    FBtr0072212 ; FBpp0072121 ; FBgn0263006 . [P22700-1 ]
    FBtr0072213 ; FBpp0072122 ; FBgn0263006 . [P22700-1 ]
    FBtr0072214 ; FBpp0072123 ; FBgn0263006 . [P22700-1 ]
    FBtr0072216 ; FBpp0072125 ; FBgn0263006 . [P22700-1 ]
    FBtr0072217 ; FBpp0072126 ; FBgn0263006 . [P22700-1 ]
    FBtr0072218 ; FBpp0072127 ; FBgn0263006 . [P22700-1 ]
    GeneIDi 49297.
    KEGGi dme:Dmel_CG3725.

    Organism-specific databases

    CTDi 49297.
    FlyBasei FBgn0263006. Ca-P60A.

    Phylogenomic databases

    eggNOGi COG0474.
    GeneTreei ENSGT00560000076887.
    InParanoidi P22700.
    OMAi PKMEDMI.
    OrthoDBi EOG73Z2SF.
    PhylomeDBi P22700.

    Miscellaneous databases

    GenomeRNAii 49297.
    NextBioi 839728.
    PROi P22700.

    Gene expression databases

    Bgeei P22700.

    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.
    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 chromosomal localization of a sarco/endoplasmic reticulum-type Ca2(+)-ATPase of Drosophila melanogaster."
      Magyar A., Varadi A.
      Biochem. Biophys. Res. Commun. 173:872-877(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Strain: Berkeley.
      Tissue: Head.
    5. "Amplification of the phosphorylation site-ATP-binding site cDNA fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by polymerase chain reaction."
      Varadi A., Gilmore-Heber M., Benz E.J. Jr.
      FEBS Lett. 258:203-207(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 357-513.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.
    7. "Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames."
      Magny E.G., Pueyo J.I., Pearl F.M., Cespedes M.A., Niven J.E., Bishop S.A., Couso J.P.
      Science 341:1116-1120(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCLA AND SCLB, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiATC1_DROME
    AccessioniPrimary (citable) accession number: P22700
    Secondary accession number(s): A4UZU0
    , Q2MGN2, Q95TX1, Q9W1G2, Q9W1G3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3