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O23087 (ECA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase 2, endoplasmic reticulum-type
EC=3.6.3.8
Gene names
Name:ECA2
Synonyms:ACA5
Ordered Locus Names:At4g00900
ORF Names:A_TM018A10.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1054 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to an endomembrane compartment.

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10541054Calcium-transporting ATPase 2, endoplasmic reticulum-type
PRO_0000046406

Regions

Topological domain1 – 5353Cytoplasmic Potential
Transmembrane54 – 7421Helical; Potential
Topological domain75 – 9824Lumenal Potential
Transmembrane99 – 11820Helical; Potential
Topological domain119 – 262144Cytoplasmic Potential
Transmembrane263 – 28220Helical; Potential
Topological domain283 – 31230Lumenal Potential
Transmembrane313 – 33018Helical; Potential
Topological domain331 – 782452Cytoplasmic Potential
Transmembrane783 – 80220Helical; Potential
Topological domain803 – 81210Lumenal Potential
Transmembrane813 – 83321Helical; Potential
Topological domain834 – 85320Cytoplasmic Potential
Transmembrane854 – 87623Helical; Potential
Topological domain877 – 94973Lumenal Potential
Transmembrane950 – 96920Helical; Potential
Topological domain970 – 98213Cytoplasmic Potential
Transmembrane983 – 100119Helical; Potential
Topological domain1002 – 101615Lumenal Potential
Transmembrane1017 – 103721Helical; Potential
Topological domain1038 – 105417Cytoplasmic Potential

Sites

Active site36814-aspartylphosphate intermediate By similarity
Metal binding3211Calcium 2; via carbonyl oxygen By similarity
Metal binding3221Calcium 2; via carbonyl oxygen By similarity
Metal binding3241Calcium 2; via carbonyl oxygen By similarity
Metal binding3261Calcium 2 By similarity
Metal binding7271Magnesium By similarity
Metal binding7311Magnesium By similarity
Metal binding7931Calcium 1 By similarity
Metal binding7961Calcium 1 By similarity
Metal binding8211Calcium 2 By similarity
Metal binding8241Calcium 1 By similarity
Metal binding8251Calcium 1 By similarity
Metal binding8251Calcium 2 By similarity
Metal binding9601Calcium 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
O23087 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B0D7F7237A3496AF

FASTA1,054115,830
        10         20         30         40         50         60 
MEEEKSFSAW SWSVEQCLKE YKTRLDKGLT SEDVQIRRQK YGFNELAKEK GKPLWHLVLE 

        70         80         90        100        110        120 
QFDDTLVKIL LGAAFISFVL AFLGEEHGSG SGFEAFVEPF VIVLILILNA VVGVWQESNA 

       130        140        150        160        170        180 
EKALEALKEM QCESAKVLRD GNVLPNLPAR ELVPGDIVEL NVGDKVPADM RVSGLKTSTL 

       190        200        210        220        230        240 
RVEQSSLTGE AMPVLKGANL VVMDDCELQG KENMVFAGTT VVNGSCVCIV TSIGMDTEIG 

       250        260        270        280        290        300 
KIQRQIHEAS LEESETPLKK KLDEFGSRLT TAICIVCVLV WMINYKNFVS WDVVDGYKPV 

       310        320        330        340        350        360 
NIKFSFEKCT YYFKIAVALA VAAIPEGLPA VITTCLALGT RKMAQKNAIV RKLPSVETLG 

       370        380        390        400        410        420 
CTTVICSDKT GTLTTNQMSA TEFFTLGGKT TTTRVFSVSG TTYDPKDGGI VDWGCNNMDA 

       430        440        450        460        470        480 
NLQAVAEICS ICNDAGVFYE GKLFRATGLP TEAALKVLVE KMGIPEKKNS ENIEEVTNFS 

       490        500        510        520        530        540 
DNGSSVKLAC CDWWNKRSKK VATLEFDRVR KSMSVIVSEP NGQNRLLVKG AAESILERSS 

       550        560        570        580        590        600 
FAQLADGSLV ALDESSREVI LKKHSEMTSK GLRCLGLAYK DELGEFSDYS SEEHPSHKKL 

       610        620        630        640        650        660 
LDPSSYSNIE TNLIFVGVVG LRDPPREEVG RAIEDCRDAG IRVMVITGDN KSTAEAICCE 

       670        680        690        700        710        720 
IRLFSENEDL SQSSFTGKEF MSLPASRRSE ILSKSGGKVF SRAEPRHKQE IVRMLKEMGE 

       730        740        750        760        770        780 
IVAMTGDGVN DAPALKLADI GIAMGITGTE VAKEASDMVL ADDNFSTIVS AVAEGRSIYN 

       790        800        810        820        830        840 
NMKAFIRYMI SSNVGEVISI FLTAALGIPE CMIPVQLLWV NLVTDGPPAT ALGFNPADID 

       850        860        870        880        890        900 
IMKKPPRKSD DCLIDSWVLI RYLVIGSYVG VATVGIFVLW YTQASFLGIS LISDGHTLVS 

       910        920        930        940        950        960 
FTQLQNWSEC SSWGTNFTAT PYTVAGGLRT IAFENNPCDY FTLGKVKPMT LSLTVLVAIE 

       970        980        990       1000       1010       1020 
MFNSLNALSE DNSLLTMPPW RNPWLLVAMT VSFALHCVIL YVPFLANVFG IVPLSFREWF 

      1030       1040       1050 
VVILVSFPVI LIDEALKFIG RCRRTRIKKK IKTM

« Hide

References

« Hide 'large scale' references
[1]"Two additional type IIA Ca(2+)-ATPases are expressed in Arabidopsis thaliana: evidence that type IIA sub-groups exist."
Pittman J.K., Mills R.F., O'Connor C.D., Williams L.E.
Gene 236:137-147(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ132387 mRNA. Translation: CAA10659.1.
AF013294 Genomic DNA. Translation: AAB62850.1.
AL161472 Genomic DNA. Translation: CAB80899.1.
CP002687 Genomic DNA. Translation: AEE81953.1.
IPIIPI00524443.
PIRT01556.
RefSeqNP_191999.1. NM_116317.3.
UniGeneAt.488.

3D structure databases

ProteinModelPortalO23087.
SMRO23087. Positions 28-388, 578-808.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-8065871.

Proteomic databases

PaxDbO23087.
PRIDEO23087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G00900.1; AT4G00900.1; AT4G00900.
GeneID827984.
KEGGath:AT4G00900.

Organism-specific databases

TAIRAt4g00900.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265621.
InParanoidO23087.
KOK01537.
OMAVDGDPME.
PhylomeDBO23087.
ProtClustDBCLSN2686070.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14601.

Gene expression databases

ArrayExpressO23087.
GenevestigatorO23087.
GermOnlineAT4G00900. Arabidopsis thaliana.

Family and domain databases

Gene3D1.20.1110.10. 3 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. 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]
PANTHERPTHR24093. PTHR24093. 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.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECA2_ARATH
AccessionPrimary (citable) accession number: O23087
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: May 29, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents