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Reviewed, UniProtKB/Swiss-Prot Q9M2L4 (ACA11_ARATH)

Last modified February 9, 2010. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Putative calcium-transporting ATPase 11, plasma membrane-type
    EC=3.6.3.8
Alternative name(s):
    Ca(2+)-ATPase isoform 11
Gene names
Name: ACA11
Ordered Locus Names: At3g57330
ORF Names: F28O9.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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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 or into organelles By similarity.

Catalytic activity

ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).

Enzyme regulation

Activated by calmodulin By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

The N-terminus contains an autoinhibitory calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion By similarity.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IIB subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Putative calcium-transporting ATPase 11, plasma membrane-type
PRO_0000046417

Regions

Topological domain1 – 157157Cytoplasmic Potential
Transmembrane158 – 17821 Potential
Topological domain179 – 19618Lumenal Potential
Transmembrane197 – 21721 Potential
Topological domain218 – 345128Cytoplasmic Potential
Transmembrane346 – 36520 Potential
Topological domain366 – 39530Lumenal Potential
Transmembrane396 – 41318 Potential
Topological domain414 – 801388Cytoplasmic Potential
Transmembrane802 – 82019 Potential
Topological domain821 – 83111Lumenal Potential
Transmembrane832 – 85221 Potential
Topological domain853 – 87220Cytoplasmic Potential
Transmembrane873 – 89523 Potential
Topological domain896 – 90712Lumenal Potential
Transmembrane908 – 92922 Potential
Topological domain930 – 94718Cytoplasmic Potential
Transmembrane948 – 96922 Potential
Topological domain970 – 97910Lumenal Potential
Transmembrane980 – 100122 Potential
Topological domain1002 – 102524Cytoplasmic Potential
Region19 – 3012Interaction with calmodulin Probable

Sites

Active site45114-aspartylphosphate intermediate By similarity
Metal binding7461Magnesium By similarity
Metal binding7501Magnesium By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9M2L4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5488C4046D7F308F

FASTA1,025111,945
        10         20         30         40         50         60 
MSNLLKDFEV ASKNPSLEAR QRWRSSVGLV KNRARRFRMI SNLDKLAENE KKRCQIQEKI 

        70         80         90        100        110        120 
RVVFYVQKAA FQFIDAGARP EYKLTDEVKK AGFYVEADEL ASMVRNHDTK SLTKIGGPEG 

       130        140        150        160        170        180 
IAQKVSVSLA EGVRSSELHI REKIYGENRY TEKPARSFLT FVWEALQDIT LIILMVCAVV 

       190        200        210        220        230        240 
SIGVGVATEG FPKGMYDGTG ILLSIILVVM VTAISDYKQS LQFRDLDREK KKIIIQVTRD 

       250        260        270        280        290        300 
GSRQEVSIHD LVVGDVVHLS IGDQVPADGI FISGYNLEID ESSLSGESEP SHVNKEKPFL 

       310        320        330        340        350        360 
LSGTKVQNGS AKMLVTTVGM RTEWGKLMDT LSEGGEDETP LQVKLNGVAT IIGKIGLGFA 

       370        380        390        400        410        420 
VLTFVVLCIR FVVEKATAGS ITEWSSEDAL TLLDYFAIAV TIIVVAVPEG LPLAVTLSLA 

       430        440        450        460        470        480 
FAMKQLMSDR ALVRHLAACE TMGSSTCICT DKTGTLTTNH MVVNKVWICE NIKERQEENF 

       490        500        510        520        530        540 
QLNLSEQVKN ILIQAIFQNT GSEVVKDKEG KTQILGSPTE RAILEFGLLL GGDVDTQRRE 

       550        560        570        580        590        600 
HKILKIEPFN SDKKKMSVLT SHSGGKVRAF CKGASEIVLK MCEKVVDSNG ESVPLSEEKI 

       610        620        630        640        650        660 
ASISDVIEGF ASEALRTLCL VYTDLDEAPR GDLPNGGYTL VAVVGIKDPV RPGVREAVQT 

       670        680        690        700        710        720 
CQAAGITVRM VTGDNISTAK AIAKECGILT AGGVAIEGSD FRNLPPHEMR AILPKIQVMA 

       730        740        750        760        770        780 
RSLPLDKHTL VNNLRKMGEV VAVTGDGTND APALHEADIG LAMGIAGTEV AKENADVIIM 

       790        800        810        820        830        840 
DDNFATIVNV AKWGRAVYIN IQKFVQFQLT VNVVALIINF VSACITGSAP LTAVQLLWVN 

       850        860        870        880        890        900 
MIMDTLGALA LATEPPNEGL MKRQPIGRTA SFITRAMWRN IIGQSIYQLI VLGILNFAGK 

       910        920        930        940        950        960 
QILNLNGPDS TIVLNTIIFN SFVFCQVFNE VNSREIEKIN VFEGMFKSWV FVAVMTATVG 

       970        980        990       1000       1010       1020 
FQVIIVEFLG AFASTVPLSW QHWLLCILIG SVSMILAVGL KCIPVESNRH HDGYELLPSG 


PSDSA

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References

[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL137080 Genomic DNA. Translation: CAB68139.1.
IPIIPI00542785.
PIRT45811.
RefSeqNP_191292.1.
UniGeneAt.34841
Rra.10508
Rra.25478

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9M2L4.

Genome annotation databases

GeneID824900.
GenomeReviewsGene locus AT3G57330 in contig BA000014_GR.
KEGGath:AT3G57330.
NMPDRfig|3702.1.peg.17065.

Organism-specific databases

TAIRAt3g57330.

Phylogenomic databases

eggNOGKOG0204.
HOGENOMHBG456486.
InParanoidQ9M2L4.
OMAEDSDTHE.
PhylomeDBQ9M2L4.

Enzyme and pathway databases

BRENDA3.6.3.8. 302.

Gene expression databases

ArrayExpressQ9M2L4.
GenevestigatorQ9M2L4.
GermOnlineAT3G57330. Arabidopsis thaliana.

Family and domain databases

InterProIPR008250. 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.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameACA11_ARATH
AccessionPrimary (citable) accession number: Q9M2L4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents