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Protein

Calcium-transporting ATPase PAT1

Gene

patA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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
Complete GO annotation...

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 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0277861. patA.

Subcellular locationi

  1. Contractile vacuole membrane; Multi-pass membrane protein
  2. Cell membrane; Multi-pass membrane protein

  3. 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9999StromalSequence AnalysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence AnalysisAdd
BLAST
Topological domaini121 – 1266LumenalSequence Analysis
Transmembranei127 – 14721HelicalSequence AnalysisAdd
BLAST
Topological domaini148 – 23588StromalSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Topological domaini257 – 28731LumenalSequence AnalysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Topological domaini309 – 32820StromalSequence AnalysisAdd
BLAST
Transmembranei329 – 34921HelicalSequence AnalysisAdd
BLAST
Topological domaini350 – 735386LumenalSequence AnalysisAdd
BLAST
Transmembranei736 – 75621HelicalSequence AnalysisAdd
BLAST
Topological domaini757 – 83276StromalSequence AnalysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence AnalysisAdd
BLAST
Topological domaini854 – 87320LumenalSequence AnalysisAdd
BLAST
Transmembranei874 – 89421HelicalSequence AnalysisAdd
BLAST
Topological domaini895 – 91319StromalSequence AnalysisAdd
BLAST
Transmembranei914 – 93421HelicalSequence AnalysisAdd
BLAST
Topological domaini935 – 9439LumenalSequence Analysis
Transmembranei944 – 96421HelicalSequence AnalysisAdd
BLAST
Topological domaini965 – 1115151StromalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
InParanoidiP54678.
KOiK01537.
OMAiSHEMESI.
PhylomeDBiP54678.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[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

        10         20         30         40         50
MTGSHEMESI MLDSMEEEFP VSVETLGKLV DVPKGFDTYA ELGGLSGLST
60 70 80 90 100
KLKSNIKTGL PLEKSSTEEN RVLKYSKNIL PDPPHQPLWS IVLDALSDHI
110 120 130 140 150
LILLIVAAVV SIVLGSIDYT SDHPETGWID GVAILVAVIL VVGITSLNDF
160 170 180 190 200
KNQARFRELN DKSNDKEVKG IRGGEQCQIS IFDVKVGDII SLDTGDIICA
210 220 230 240 250
DGVFIEGHAL KCDESSITGE SDPIKKGQPQ DNMDPFLISG SMVIEGFGTM
260 270 280 290 300
LVTAVGVNSF NGKTMMGLRV ASEDTPLQMK LSVLASRIGY FGMGAAILML
310 320 330 340 350
LIAIPKYFIQ RKVHDIEITR EDAQPIVQLV ISAITIVVVA VPEGLPLAVT
360 370 380 390 400
MALAYGMMKM FKENNLVRNL ASCETMGSAT TICSDKTGTL TQNVMSVVTG
410 420 430 440 450
TICGVFPTLD GIAQKIPKHV QSILTDGMAI NSNAYEGVSS KGKLEFIGSK
460 470 480 490 500
TECALLNFGK LFGCDYNEVR KRLEVVELYP FSSARKRMSV LVKHDQNLRL
510 520 530 540 550
FTKGASEIIL GQCGSYLDEA GNIRPISEAK AYFEEQINNF ASDALRTIGL
560 570 580 590 600
AYRDFQYGEC DFKEPPENNL VFIGIVGIKD PLRPEVPEAV EICKRAGIVV
610 620 630 640 650
RMVTGDNLVT AQNIARNCGI LTEGGLCMEG PKFRELSQSE MDAILPKLQV
660 670 680 690 700
LARSSPTDKQ LLVGRLKDLG EVVAVTGDGT NDGPALKLAN VGFSMGISGT
710 720 730 740 750
EVAIAASDVV LLDDNFASIV RAVLWGRNIY DAICKFLQFQ LTVNVVAVTV
760 770 780 790 800
AFIGTLTSDV VEDKDNSSSS GSADKVTEEE PRQGSPLTAV QLLWVNLIMD
810 820 830 840 850
TLAALALATE PPTPELLERP PNGKNAPLIT RSMWKNIIGQ AALQLAILFT
860 870 880 890 900
ILYQGHNIFQ HFVPQAHGPI IKNGLHHYTL VFNCFVFLQL FNEINARVLG
910 920 930 940 950
SRTNPFKNFF NNPIFIAVMI FTLGVQIIFV TFGGSATSTD SLYIVEWICC
960 970 980 990 1000
VVVGAISLPV GLLLRKIPIR EPVVKNEIPV HSEAVYTSPS PNPSSSNLLG
1010 1020 1030 1040 1050
SGGAKPISKD YPTSGESTPP INDEGSPLVT RKTSVGASAN DNINTPIPSS
1060 1070 1080 1090 1100
SSNLVNLNKP TQVGRGWQIV RQTHKKLVVI NALKEFSQNK EPGLVDVVRG
1110
TNRGSLHLPV NQINN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X89369 mRNA. Translation: CAA61551.1.
AAFI02000023 Genomic DNA. Translation: EAL68103.2.
PIRiS57726.
RefSeqiXP_642164.2. XM_637072.2.

3D structure databases

ProteinModelPortaliP54678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0214945.

Protein family/group databases

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

Proteomic databases

PRIDEiP54678.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

dictyBaseiDDB_G0277861. patA.

Phylogenomic databases

eggNOGiCOG0474.
InParanoidiP54678.
KOiK01537.
OMAiSHEMESI.
PhylomeDBiP54678.

Miscellaneous databases

PROiP54678.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.