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P54678

- ATC1_DICDI

UniProt

P54678 - ATC1_DICDI

Protein

Calcium-transporting ATPase PAT1

Gene

patA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
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    Functioni

    Calcium ATPase involved in Ca2+ homeostasis as a component of the contractile vacuole complex.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei385 – 38514-aspartylphosphate intermediateBy similarity
    Metal bindingi678 – 6781MagnesiumBy similarity
    Metal bindingi682 – 6821MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: dictyBase
    2. calcium ion binding Source: dictyBase
    3. calcium ion transmembrane transporter activity Source: dictyBase
    4. calcium-transporting ATPase activity Source: UniProtKB

    GO - Biological processi

    1. calcium ion transport Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

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

    Protein family/group databases

    TCDBi3.A.3.2.17. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium-transporting ATPase PAT1 (EC:3.6.3.8)
    Gene namesi
    Name:patA
    ORF Names:DDB_G0277861
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0277861. patA.

    Subcellular locationi

    Contractile vacuole membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein
    Note: Contractile vacuole complex. Localizes to the contractile vacule membrane in unstimulated cells. Localizes to the cell membrane and the contractile vacule membrane in cells stimulated by calcium.

    GO - Cellular componenti

    1. contractile vacuolar membrane Source: UniProtKB
    2. integral component of membrane Source: dictyBase
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11151115Calcium-transporting ATPase PAT1PRO_0000046179Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP54678.

    Expressioni

    Developmental stagei

    Expressed constitutively at very low levels during vegetative growth and throughout development.1 Publication

    Inductioni

    By calcium.2 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0214945.

    Structurei

    3D structure databases

    ProteinModelPortaliP54678.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9999StromalSequence AnalysisAdd
    BLAST
    Topological domaini121 – 1266LumenalSequence Analysis
    Topological domaini148 – 23588StromalSequence AnalysisAdd
    BLAST
    Topological domaini257 – 28731LumenalSequence AnalysisAdd
    BLAST
    Topological domaini309 – 32820StromalSequence AnalysisAdd
    BLAST
    Topological domaini350 – 735386LumenalSequence AnalysisAdd
    BLAST
    Topological domaini757 – 83276StromalSequence AnalysisAdd
    BLAST
    Topological domaini854 – 87320LumenalSequence AnalysisAdd
    BLAST
    Topological domaini895 – 91319StromalSequence AnalysisAdd
    BLAST
    Topological domaini935 – 9439LumenalSequence Analysis
    Topological domaini965 – 1115151StromalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei100 – 12021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei127 – 14721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei236 – 25621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei288 – 30821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei329 – 34921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei736 – 75621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei833 – 85321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei874 – 89421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei914 – 93421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei944 – 96421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    KOiK01537.
    OMAiSHEMESI.
    PhylomeDBiP54678.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR006408. ATPase_P-typ_Ca-transp_plasma.
    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. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54678-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGSHEMESI MLDSMEEEFP VSVETLGKLV DVPKGFDTYA ELGGLSGLST     50
    KLKSNIKTGL PLEKSSTEEN RVLKYSKNIL PDPPHQPLWS IVLDALSDHI 100
    LILLIVAAVV SIVLGSIDYT SDHPETGWID GVAILVAVIL VVGITSLNDF 150
    KNQARFRELN DKSNDKEVKG IRGGEQCQIS IFDVKVGDII SLDTGDIICA 200
    DGVFIEGHAL KCDESSITGE SDPIKKGQPQ DNMDPFLISG SMVIEGFGTM 250
    LVTAVGVNSF NGKTMMGLRV ASEDTPLQMK LSVLASRIGY FGMGAAILML 300
    LIAIPKYFIQ RKVHDIEITR EDAQPIVQLV ISAITIVVVA VPEGLPLAVT 350
    MALAYGMMKM FKENNLVRNL ASCETMGSAT TICSDKTGTL TQNVMSVVTG 400
    TICGVFPTLD GIAQKIPKHV QSILTDGMAI NSNAYEGVSS KGKLEFIGSK 450
    TECALLNFGK LFGCDYNEVR KRLEVVELYP FSSARKRMSV LVKHDQNLRL 500
    FTKGASEIIL GQCGSYLDEA GNIRPISEAK AYFEEQINNF ASDALRTIGL 550
    AYRDFQYGEC DFKEPPENNL VFIGIVGIKD PLRPEVPEAV EICKRAGIVV 600
    RMVTGDNLVT AQNIARNCGI LTEGGLCMEG PKFRELSQSE MDAILPKLQV 650
    LARSSPTDKQ LLVGRLKDLG EVVAVTGDGT NDGPALKLAN VGFSMGISGT 700
    EVAIAASDVV LLDDNFASIV RAVLWGRNIY DAICKFLQFQ LTVNVVAVTV 750
    AFIGTLTSDV VEDKDNSSSS GSADKVTEEE PRQGSPLTAV QLLWVNLIMD 800
    TLAALALATE PPTPELLERP PNGKNAPLIT RSMWKNIIGQ AALQLAILFT 850
    ILYQGHNIFQ HFVPQAHGPI IKNGLHHYTL VFNCFVFLQL FNEINARVLG 900
    SRTNPFKNFF NNPIFIAVMI FTLGVQIIFV TFGGSATSTD SLYIVEWICC 950
    VVVGAISLPV GLLLRKIPIR EPVVKNEIPV HSEAVYTSPS PNPSSSNLLG 1000
    SGGAKPISKD YPTSGESTPP INDEGSPLVT RKTSVGASAN DNINTPIPSS 1050
    SSNLVNLNKP TQVGRGWQIV RQTHKKLVVI NALKEFSQNK EPGLVDVVRG 1100
    TNRGSLHLPV NQINN 1115
    Length:1,115
    Mass (Da):120,677
    Last modified:December 4, 2007 - v2
    Checksum:i6A80A21D490973AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121C → Y in CAA61551. (PubMed:7499325)Curated
    Sequence conflicti277 – 2771L → H in CAA61551. (PubMed:7499325)Curated
    Sequence conflicti289 – 2902GY → WL in CAA61551. (PubMed:7499325)Curated
    Sequence conflicti344 – 3441G → V in CAA61551. (PubMed:7499325)Curated
    Sequence conflicti643 – 6431A → V in CAA61551. (PubMed:7499325)Curated
    Sequence conflicti680 – 6801T → S in CAA61551. (PubMed:7499325)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89369 mRNA. Translation: CAA61551.1.
    AAFI02000023 Genomic DNA. Translation: EAL68103.2.
    PIRiS57726.
    RefSeqiXP_642164.2. XM_637072.2.

    Genome annotation databases

    EnsemblProtistsiDDB0214945; DDB0214945; DDB_G0277861.
    GeneIDi8621371.
    KEGGiddi:DDB_G0277861.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89369 mRNA. Translation: CAA61551.1 .
    AAFI02000023 Genomic DNA. Translation: EAL68103.2 .
    PIRi S57726.
    RefSeqi XP_642164.2. XM_637072.2.

    3D structure databases

    ProteinModelPortali P54678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0214945.

    Protein family/group databases

    TCDBi 3.A.3.2.17. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    PRIDEi P54678.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0214945 ; DDB0214945 ; DDB_G0277861 .
    GeneIDi 8621371.
    KEGGi ddi:DDB_G0277861.

    Organism-specific databases

    dictyBasei DDB_G0277861. patA.

    Phylogenomic databases

    eggNOGi COG0474.
    KOi K01537.
    OMAi SHEMESI.
    PhylomeDBi P54678.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR006408. ATPase_P-typ_Ca-transp_plasma.
    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. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01517. ATPase-IIB_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of an intracellular P-type ATPase from Dictyostelium that is up-regulated in calcium-adapted cells."
      Moniakis J., Coukell M.B., Forer A.
      J. Biol. Chem. 270:28276-28281(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: AX3.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Involvement of the Ca2+-ATPase PAT1 and the contractile vacuole in calcium regulation in Dictyostelium discoideum."
      Moniakis J., Coukell M.B., Janiec A.
      J. Cell Sci. 112:405-414(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.

    Entry informationi

    Entry nameiATC1_DICDI
    AccessioniPrimary (citable) accession number: P54678
    Secondary accession number(s): Q54YN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    Loss-of-function mutant (antisense inhibition) displays impaired growth in high Ca2+ medium but normal growth in low Ca2+ medium. Antisense inhibition does not affect development in high Ca2+ medium.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3