Calcium-transporting ATPase PAT1 - Dictyostelium discoideum (Slime mold)

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P54678 (ATC1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Calcium-transporting ATPase PAT1
EC=3.6.3.8

Gene names

Name:	patA
ORF Names:	DDB_G0277861

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1115 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Calcium ATPase involved in Ca²⁺ homeostasis as a component of the contractile vacuole complex. Ref.1 Ref.3
Catalytic activity	ATP + H₂O + Ca²⁺[side 1] = ADP + phosphate + Ca²⁺[side 2].
Subcellular location	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. Ref.1 Ref.3
Developmental stage	Expressed constitutively at very low levels during vegetative growth and throughout development. Ref.1
Induction	By calcium. Ref.1 Ref.3
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.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane Vacuole
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	contractile vacuolar membrane Inferred from direct assay Ref.3. Source: UniProtKB integral to membrane Traceable author statement Ref.1. Source: dictyBase plasma membrane Inferred from direct assay Ref.3. Source: UniProtKB
Molecular function	ATP binding Traceable author statement Ref.1. Source: dictyBase calcium ion binding Traceable author statement Ref.1. Source: dictyBase calcium-transporting ATPase activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1115

1115

Calcium-transporting ATPase PAT1

PRO_0000046179

Regions

Topological domain

1 – 99

Stromal Potential

Transmembrane

100 – 120

Helical; Potential

Topological domain

121 – 126

Lumenal Potential

Transmembrane

127 – 147

Helical; Potential

Topological domain

148 – 235

Stromal Potential

Transmembrane

236 – 256

Helical; Potential

Topological domain

257 – 287

Lumenal Potential

Transmembrane

288 – 308

Helical; Potential

Topological domain

309 – 328

Stromal Potential

Transmembrane

329 – 349

Helical; Potential

Topological domain

350 – 735

386

Lumenal Potential

Transmembrane

736 – 756

Helical; Potential

Topological domain

757 – 832

Stromal Potential

Transmembrane

833 – 853

Helical; Potential

Topological domain

854 – 873

Lumenal Potential

Transmembrane

874 – 894

Helical; Potential

Topological domain

895 – 913

Stromal Potential

Transmembrane

914 – 934

Helical; Potential

Topological domain

935 – 943

Lumenal Potential

Transmembrane

944 – 964

Helical; Potential

Topological domain

965 – 1115

151

Stromal Potential

Sites

Active site

385

4-aspartylphosphate intermediate By similarity

Metal binding

678

Magnesium By similarity

Metal binding

682

Magnesium By similarity

Experimental info

Sequence conflict

212

C → Y in CAA61551. Ref.1

Sequence conflict

277

L → H in CAA61551. Ref.1

Sequence conflict

289 – 290

GY → WL in CAA61551. Ref.1

Sequence conflict

344

G → V in CAA61551. Ref.1

Sequence conflict

643

A → V in CAA61551. Ref.1

Sequence conflict

680

T → S in CAA61551. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P54678 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 6A80A21D490973AB
Show »

FASTA

1,115

120,677

        10         20         30         40         50         60 
MTGSHEMESI MLDSMEEEFP VSVETLGKLV DVPKGFDTYA ELGGLSGLST KLKSNIKTGL 

        70         80         90        100        110        120 
PLEKSSTEEN RVLKYSKNIL PDPPHQPLWS IVLDALSDHI LILLIVAAVV SIVLGSIDYT 

       130        140        150        160        170        180 
SDHPETGWID GVAILVAVIL VVGITSLNDF KNQARFRELN DKSNDKEVKG IRGGEQCQIS 

       190        200        210        220        230        240 
IFDVKVGDII SLDTGDIICA DGVFIEGHAL KCDESSITGE SDPIKKGQPQ DNMDPFLISG 

       250        260        270        280        290        300 
SMVIEGFGTM LVTAVGVNSF NGKTMMGLRV ASEDTPLQMK LSVLASRIGY FGMGAAILML 

       310        320        330        340        350        360 
LIAIPKYFIQ RKVHDIEITR EDAQPIVQLV ISAITIVVVA VPEGLPLAVT MALAYGMMKM 

       370        380        390        400        410        420 
FKENNLVRNL ASCETMGSAT TICSDKTGTL TQNVMSVVTG TICGVFPTLD GIAQKIPKHV 

       430        440        450        460        470        480 
QSILTDGMAI NSNAYEGVSS KGKLEFIGSK TECALLNFGK LFGCDYNEVR KRLEVVELYP 

       490        500        510        520        530        540 
FSSARKRMSV LVKHDQNLRL FTKGASEIIL GQCGSYLDEA GNIRPISEAK AYFEEQINNF 

       550        560        570        580        590        600 
ASDALRTIGL AYRDFQYGEC DFKEPPENNL VFIGIVGIKD PLRPEVPEAV EICKRAGIVV 

       610        620        630        640        650        660 
RMVTGDNLVT AQNIARNCGI LTEGGLCMEG PKFRELSQSE MDAILPKLQV LARSSPTDKQ 

       670        680        690        700        710        720 
LLVGRLKDLG EVVAVTGDGT NDGPALKLAN VGFSMGISGT EVAIAASDVV LLDDNFASIV 

       730        740        750        760        770        780 
RAVLWGRNIY DAICKFLQFQ LTVNVVAVTV AFIGTLTSDV VEDKDNSSSS GSADKVTEEE 

       790        800        810        820        830        840 
PRQGSPLTAV QLLWVNLIMD TLAALALATE PPTPELLERP PNGKNAPLIT RSMWKNIIGQ 

       850        860        870        880        890        900 
AALQLAILFT ILYQGHNIFQ HFVPQAHGPI IKNGLHHYTL VFNCFVFLQL FNEINARVLG 

       910        920        930        940        950        960 
SRTNPFKNFF NNPIFIAVMI FTLGVQIIFV TFGGSATSTD SLYIVEWICC VVVGAISLPV 

       970        980        990       1000       1010       1020 
GLLLRKIPIR EPVVKNEIPV HSEAVYTSPS PNPSSSNLLG SGGAKPISKD YPTSGESTPP 

      1030       1040       1050       1060       1070       1080 
INDEGSPLVT RKTSVGASAN DNINTPIPSS SSNLVNLNKP TQVGRGWQIV RQTHKKLVVI 

      1090       1100       1110 
NALKEFSQNK EPGLVDVVRG TNRGSLHLPV NQINN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7499325] [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. Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [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: 9885293] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89369 mRNA. Translation: CAA61551.1. AAFI02000023 Genomic DNA. Translation: EAL68103.2.
PIR	S57726.
RefSeq	XP_642164.2. XM_637072.2.
3D structure databases
ProteinModelPortal	P54678.
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.2.17. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PRIDE	P54678.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0214945; DDB0214945; DDB_G0277861.
GeneID	8621371.
GenomeReviews	Gene locus patA in contig CM000152_GR.
KEGG	ddi:DDB_G0277861.
Organism-specific databases
dictyBase	DDB_G0277861. patA.
Phylogenomic databases
eggNOG	KOG0204.
GeneTree	EPrGT00050000000458.
HOGENOM	HBG456486.
OMA	SANDNIN.
PhylomeDB	P54678.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006408. ATPase_P-typ_Ca-transp_PMCA. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 1 hit.
KO	K01537.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01517. ATPase-IIB_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATC1_DICDI

Accession

Primary (citable) accession number: P54678
Secondary accession number(s): Q54YN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents