Calcium-transporting ATPase 8, plasma membrane-type - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (?) or add your own

Q9LF79 (ACA8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Calcium-transporting ATPase 8, plasma membrane-type
EC=3.6.3.8

Alternative name(s):
Ca(2+)-ATPase isoform 8

Gene names

Name:	ACA8
Ordered Locus Names:	At5g57110
ORF Names:	MUL3.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1074 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell.
Catalytic activity	ATP + H₂O + Ca²⁺(Side 1) = ADP + phosphate + Ca²⁺(Side 2).
Enzyme regulation	Activated by calmodulin By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Domain	The N-terminus contains an autoinhibitory calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion. Ref.1
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]
Sequence caution	The sequence BAA97361.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Calmodulin-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to nematode Inferred from expression pattern PubMed 16478044. Source: TAIR
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.1 Ref.5 PubMed 16618929 PubMed 17317660 PubMed 17644812 PubMed 22923678. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Inferred from direct assay PubMed 14648121. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein self-association Inferred from direct assay PubMed 15358533. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CALM	P62157	14	EBI-980643,EBI-397403	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1074

1074

Calcium-transporting ATPase 8, plasma membrane-type

PRO_0000046414

Regions

Topological domain

1 – 180

180

Cytoplasmic Potential

Transmembrane

181 – 201

Helical; Potential

Topological domain

202 – 219

Extracellular Potential

Transmembrane

220 – 240

Helical; Potential

Topological domain

241 – 369

129

Cytoplasmic Potential

Transmembrane

370 – 389

Helical; Potential

Topological domain

390 – 426

Extracellular Potential

Transmembrane

427 – 444

Helical; Potential

Topological domain

445 – 840

396

Cytoplasmic Potential

Transmembrane

841 – 859

Helical; Potential

Topological domain

860 – 870

Extracellular Potential

Transmembrane

871 – 891

Helical; Potential

Topological domain

892 – 911

Cytoplasmic Potential

Transmembrane

912 – 934

Helical; Potential

Topological domain

935 – 949

Extracellular Potential

Transmembrane

950 – 971

Helical; Potential

Topological domain

972 – 989

Cytoplasmic Potential

Transmembrane

990 – 1011

Helical; Potential

Topological domain

1012 – 1021

Extracellular Potential

Transmembrane

1022 – 1043

Helical; Potential

Topological domain

1044 – 1074

Cytoplasmic Potential

Region

43 – 54

Interaction with calmodulin

Sites

Active site

482

4-aspartylphosphate intermediate By similarity

Metal binding

785

Magnesium By similarity

Metal binding

789

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.5 Ref.6

Modified residue

Phosphoserine Ref.5 Ref.6 Ref.7

Modified residue

Phosphoserine Ref.5 Ref.6 Ref.8

Modified residue

Phosphoserine Ref.5 Ref.6

Modified residue

Phosphothreonine Ref.5

Secondary structure

1074

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9LF79 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2E86572F44DEA8A5
Show »

FASTA

1,074

116,174

        10         20         30         40         50         60 
MTSLLKSSPG RRRGGDVESG KSEHADSDSD TFYIPSKNAS IERLQQWRKA ALVLNASRRF 

        70         80         90        100        110        120 
RYTLDLKKEQ ETREMRQKIR SHAHALLAAN RFMDMGRESG VEKTTGPATP AGDFGITPEQ 

       130        140        150        160        170        180 
LVIMSKDHNS GALEQYGGTQ GLANLLKTNP EKGISGDDDD LLKRKTIYGS NTYPRKKGKG 

       190        200        210        220        230        240 
FLRFLWDACH DLTLIILMVA AVASLALGIK TEGIKEGWYD GGSIAFAVIL VIVVTAVSDY 

       250        260        270        280        290        300 
KQSLQFQNLN DEKRNIHLEV LRGGRRVEIS IYDIVVGDVI PLNIGNQVPA DGVLISGHSL 

       310        320        330        340        350        360 
ALDESSMTGE SKIVNKDANK DPFLMSGCKV ADGNGSMLVT GVGVNTEWGL LMASISEDNG 

       370        380        390        400        410        420 
EETPLQVRLN GVATFIGSIG LAVAAAVLVI LLTRYFTGHT KDNNGGPQFV KGKTKVGHVI 

       430        440        450        460        470        480 
DDVVKVLTVA VTIVVVAVPE GLPLAVTLTL AYSMRKMMAD KALVRRLSAC ETMGSATTIC 

       490        500        510        520        530        540 
SDKTGTLTLN QMTVVESYAG GKKTDTEQLP ATITSLVVEG ISQNTTGSIF VPEGGGDLEY 

       550        560        570        580        590        600 
SGSPTEKAIL GWGVKLGMNF ETARSQSSIL HAFPFNSEKK RGGVAVKTAD GEVHVHWKGA 

       610        620        630        640        650        660 
SEIVLASCRS YIDEDGNVAP MTDDKASFFK NGINDMAGRT LRCVALAFRT YEAEKVPTGE 

       670        680        690        700        710        720 
ELSKWVLPED DLILLAIVGI KDPCRPGVKD SVVLCQNAGV KVRMVTGDNV QTARAIALEC 

       730        740        750        760        770        780 
GILSSDADLS EPTLIEGKSF REMTDAERDK ISDKISVMGR SSPNDKLLLV QSLRRQGHVV 

       790        800        810        820        830        840 
AVTGDGTNDA PALHEADIGL AMGIAGTEVA KESSDIIILD DNFASVVKVV RWGRSVYANI 

       850        860        870        880        890        900 
QKFIQFQLTV NVAALVINVV AAISSGDVPL TAVQLLWVNL IMDTLGALAL ATEPPTDHLM 

       910        920        930        940        950        960 
GRPPVGRKEP LITNIMWRNL LIQAIYQVSV LLTLNFRGIS ILGLEHEVHE HATRVKNTII 

       970        980        990       1000       1010       1020 
FNAFVLCQAF NEFNARKPDE KNIFKGVIKN RLFMGIIVIT LVLQVIIVEF LGKFASTTKL 

      1030       1040       1050       1060       1070 
NWKQWLICVG IGVISWPLAL VGKFIPVPAA PISNKLKVLK FWGKKKNSSG EGSL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"At-ACA8 encodes a plasma membrane-localized Ca2+-ATPase of Arabidopsis with a calmodulin-binding domain at the N-terminus." Bonza M.C., Morandini P., Luoni L., Geisler M., Palmgren M.G., De Michelis M.I. Plant Physiol. 123:1495-1506(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CALMODULIN-BINDING DOMAIN. Strain: cv. Landsberg erecta.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-22; SER-27; SER-29 AND THR-31, MASS SPECTROMETRY. Strain: cv. La-0.
[6]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-22; SER-27 AND SER-29, MASS SPECTROMETRY.
[7]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: Seedling.
[8]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ249352 mRNA. Translation: CAB96189.1.
AB023042 Genomic DNA. Translation: BAA97361.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED96847.1.
CP002688 Genomic DNA. Translation: AED96848.1.
AY069869 mRNA. Translation: AAL47426.1.

IPI

IPI00540817.

PIR

T52654.

RefSeq

NP_200521.3. NM_125093.5.
NP_851200.1. NM_180869.3.

UniGene

At.9676.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AQR	X-ray	1.95	D	40-95	[»]

ProteinModelPortal

Q9LF79.

SMR

Q9LF79. Positions 39-95, 138-1047.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9LF79. 1 interaction.

Protein family/group databases

TCDB

3.A.3.2.10. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PaxDb

Q9LF79.

PRIDE

Q9LF79.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G57110.1; AT5G57110.1; AT5G57110.
AT5G57110.2; AT5G57110.2; AT5G57110.

GeneID

835815.

KEGG

ath:AT5G57110.

Organism-specific databases

TAIR

At5g57110.

Phylogenomic databases

eggNOG

COG0474.

HOGENOM

HOG000265623.

InParanoid

Q9LF79.

OMA

FSWPLAF.

PhylomeDB

Q9LF79.

ProtClustDB

CLSN2685405.

Gene expression databases

ArrayExpress

Q9LF79.

Genevestigator

Q9LF79.

GermOnline

AT5G57110. Arabidopsis thaliana.

Family and domain databases

Gene3D

1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.

InterPro

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.
IPR024750. Ca_ATPase_N_dom.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]

PANTHER

PTHR24093. PTHR24093. 1 hit.

Pfam

PF12515. CaATP_NAI. 1 hit.
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

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACA8_ARATH

Accession

Primary (citable) accession number: Q9LF79
Secondary accession number(s): Q9LU75

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents