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Q9SY55 (ECA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase 3, endoplasmic reticulum-type

Short name=AtECA3
EC=3.6.3.8
Gene names
Name:ECA3
Synonyms:ACA6
Ordered Locus Names:At1g10130
ORF Names:F14N23.1, T27I1.16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length998 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. Involved in calcium-enhanced root growth, in tolerance to toxic levels of manganese and in secretory processes. Has a crucial role in manganese nutrition, but is not involved in transporting copper, iron or zinc. Ref.3 Ref.4

Catalytic activity

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

Subcellular location

Endosome membrane; Multi-pass membrane protein. Prevacuolar compartment membrane; Multi-pass membrane protein Ref.3 Ref.4.

Tissue specificity

Expressed in root cap, in elongation and differentiation zones of roots, in vascular tissues of roots, leaves, floral pedicels and style, in leaves, including hydathodes and guard cells, in stamens, in petals, in sepals and in siliques. Ref.3 Ref.4

Induction

Not induced by manganese or zinc. Ref.3

Miscellaneous

ECA3 is functionally distinct from ECA1 and is localized to a separate compartment.

Sequence similarities

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

Sequence caution

The sequence AAD32863.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndosome
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from mutant phenotype Ref.4. Source: GOC

calcium ion transport

Inferred from sequence or structural similarity Ref.2. Source: TAIR

manganese ion homeostasis

Inferred from mutant phenotype Ref.3. Source: TAIR

manganese ion transmembrane transport

Inferred from mutant phenotype Ref.4. Source: GOC

manganese ion transport

Inferred from genetic interaction Ref.3. Source: TAIR

root development

Inferred from mutant phenotype Ref.4. Source: TAIR

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.3PubMed 22430844PubMed 22923678. Source: TAIR

endomembrane system

Inferred from direct assay Ref.4. Source: TAIR

endosome

Inferred from direct assay PubMed 22923678. Source: TAIR

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from direct assay PubMed 22923678. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-transporting ATPase activity

Inferred from mutant phenotype Ref.4. Source: TAIR

manganese-transporting ATPase activity

Inferred from mutant phenotype Ref.4. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 998998Calcium-transporting ATPase 3, endoplasmic reticulum-type
PRO_0000046407

Regions

Topological domain1 – 4848Cytoplasmic Potential
Transmembrane49 – 6921Helical; Potential
Topological domain70 – 8920Lumenal Potential
Transmembrane90 – 10920Helical; Potential
Topological domain110 – 250141Cytoplasmic Potential
Transmembrane251 – 27020Helical; Potential
Topological domain271 – 29121Lumenal Potential
Transmembrane292 – 30918Helical; Potential
Topological domain310 – 746437Cytoplasmic Potential
Transmembrane747 – 76620Helical; Potential
Topological domain767 – 77610Lumenal Potential
Transmembrane777 – 79721Helical; Potential
Topological domain798 – 81720Cytoplasmic Potential
Transmembrane818 – 84023Helical; Potential
Topological domain841 – 88343Lumenal Potential
Transmembrane884 – 90320Helical; Potential
Topological domain904 – 91613Cytoplasmic Potential
Transmembrane917 – 93519Helical; Potential
Topological domain936 – 95015Lumenal Potential
Transmembrane951 – 97121Helical; Potential
Topological domain972 – 99827Cytoplasmic Potential

Sites

Active site34714-aspartylphosphate intermediate By similarity
Metal binding3001Calcium 2; via carbonyl oxygen By similarity
Metal binding3011Calcium 2; via carbonyl oxygen By similarity
Metal binding3031Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2 By similarity
Metal binding6921Magnesium By similarity
Metal binding6961Magnesium By similarity
Metal binding7571Calcium 1 By similarity
Metal binding7601Calcium 1 By similarity
Metal binding7851Calcium 2 By similarity
Metal binding7881Calcium 1 By similarity
Metal binding7891Calcium 1 By similarity
Metal binding7891Calcium 2 By similarity
Metal binding8941Calcium 1 By similarity

Experimental info

Sequence conflict461R → G in CAA10660. Ref.2
Sequence conflict55 – 562KQ → NS in AAD29961. Ref.1
Sequence conflict2001D → N in AAT68271. Ref.4
Sequence conflict378 – 3814TVSG → LLVE in AAD29961. Ref.1
Sequence conflict4111A → T in AAT68271. Ref.4
Sequence conflict5491S → R in CAA10660. Ref.2
Sequence conflict5861Missing in AAT68271. Ref.4
Sequence conflict7471K → R in AAD29961. Ref.1
Sequence conflict943 – 9442FS → CA in AAD29961. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9SY55 [UniParc].

Last modified September 26, 2001. Version 3.
Checksum: 214C9865833BA7C0

FASTA998109,060
        10         20         30         40         50         60 
MEDAYARSVS EVLDFFGVDP TKGLSDSQVV HHSRLYGRNV LPEEKRTPFW KLVLKQFDDL 

        70         80         90        100        110        120 
LVKILIVAAI VSFVLALANG ETGLTAFLEP FVILLILAAN AAVGVITETN AEKALEELRA 

       130        140        150        160        170        180 
YQANIATVLR NGCFSILPAT ELVPGDIVEV TVGCKIPADL RMIEMSSNTF RVDQAILTGE 

       190        200        210        220        230        240 
SCSVEKDVDC TLTTNAVYQD KKNILFSGTD VVAGRGRAVV IGVGSNTAMG SIHDSMLQTD 

       250        260        270        280        290        300 
DEATPLKKKL DEFGSFLAKV IAGICVLVWV VNIGHFSDPS HGGFFKGAIH YFKIAVALAV 

       310        320        330        340        350        360 
AAIPEGLPAV VTTCLALGTK KMARLNAIVR SLPSVETLGC TTVICSDKTG TLTTNMMSVS 

       370        380        390        400        410        420 
KICVVQSAEH GPMINEFTVS GTTYAPEGTV FDSNGMQLDL PAQSPCLHHL AMCSSLCNDS 

       430        440        450        460        470        480 
ILQYNPDKDS YEKIGESTEV ALRVLAEKVG LPGFDSMPSA LNMLSKHERA SYCNHYWENQ 

       490        500        510        520        530        540 
FKKVYVLEFT RDRKMMSVLC SHKQMDVMFS KGAPESIIAR CNKILCNGDG SVVPLTAAGR 

       550        560        570        580        590        600 
AELESRFYSF GDETLRCLAL AFKTVPHGQQ TISYDNENDL TFIGLVGMLD PPREEVRDAM 

       610        620        630        640        650        660 
LACMTAGIRV IVVTGDNKST AESLCRKIGA FDNLVDFSGM SYTASEFERL PAVQQTLALR 

       670        680        690        700        710        720 
RMTLFSRVEP SHKRMLVEAL QKQNEVVAMT GDGVNDAPAL KKADIGIAMG SGTAVAKSAS 

       730        740        750        760        770        780 
DMVLADDNFA SIVAAVAEGR AIYNNTKQFI RYMISSNIGE VVCIFVAAVL GIPDTLAPVQ 

       790        800        810        820        830        840 
LLWVNLVTDG LPATAIGFNK QDSDVMKAKP RKVGEAVVTG WLFFRYLVIG VYVGLATVAG 

       850        860        870        880        890        900 
FIWWFVYSDG GPKLTYSELM NFETCALRET TYPCSIFEDR HPSTVAMTVL VVVEMFNALN 

       910        920        930        940        950        960 
NLSENQSLLV ITPRSNLWLV GSIILTMLLH VLILYVHPLA VLFSVTPLSW AEWTAVLYLS 

       970        980        990 
FPVIIIDELL KFLSRNTGMR FRFRLRKADL LPKDRRDK 

« Hide

References

« Hide 'large scale' references
[1]"AtECA3 encodes a homolog of endoplasmic reticulum-type Ca2+-ATPase from Arabidopsis thaliana."
Liang F., Sze H.
Plant Gene Register PGR99-077
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Seedling.
[2]"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. Landsberg erecta.
[3]"ECA3, a Golgi-localized P2A-type ATPase, plays a crucial role in manganese nutrition in Arabidopsis."
Mills R.F., Doherty M.L., Lopez-Marques R.L., Weimar T., Dupree P., Palmgren M.G., Pittman J.K., Williams L.E.
Plant Physiol. 146:116-128(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[4]"A distinct endosomal Ca2+/Mn2+ pump affects root growth through the secretory process."
Li X., Chanroj S., Wu Z., Romanowsky S.M., Harper J.F., Sze H.
Plant Physiol. 147:1675-1689(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[5]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[6]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[7]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117296 mRNA. Translation: AAD29961.1.
AJ132388 mRNA. Translation: CAA10660.1.
EU082212 mRNA. Translation: ABU53680.1.
AY650902 mRNA. Translation: AAT68271.1.
AC004122 Genomic DNA. Translation: AAC34328.2.
AC005489 Genomic DNA. Translation: AAD32863.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28545.1.
AK229199 mRNA. Translation: BAF01069.1.
PIRT00633.
T52581.
RefSeqNP_563860.1. NM_100887.2.
UniGeneAt.24768.

3D structure databases

ProteinModelPortalQ9SY55.
SMRQ9SY55. Positions 1-976.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB3.A.3.2.19. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbQ9SY55.
PRIDEQ9SY55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G10130.1; AT1G10130.1; AT1G10130.
GeneID837550.
KEGGath:AT1G10130.

Organism-specific databases

TAIRAT1G10130.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265621.
InParanoidQ9SY55.
KOK01537.
OMAGSQSKMF.
PhylomeDBQ9SY55.
ProtClustDBCLSN2687751.

Enzyme and pathway databases

BioCycARA:AT1G10130-MONOMER.
MetaCyc:MONOMER-14610.

Gene expression databases

GenevestigatorQ9SY55.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR005782. ATPase_P-typ_Ca-transp_IIA.
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.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
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]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECA3_ARATH
AccessionPrimary (citable) accession number: Q9SY55
Secondary accession number(s): Q0WP80 expand/collapse secondary AC list , Q6DQH3, Q9SAV5, Q9SMX2, Q9SWS8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names