Calcium-transporting ATPase 3, endoplasmic reticulum-type - Arabidopsis thaliana (Mouse-ear cress)

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Q9SY55 (ECA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. 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 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

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	998 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Calcium transport Ion transport Transport
Cellular component	Endosome Membrane
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	manganese ion homeostasis Inferred from mutant phenotype Ref.3. Source: TAIR root development Inferred from mutant phenotype Ref.4. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay Ref.3 PubMed 22430844 PubMed 22923678. Source: TAIR endomembrane system Inferred from direct assay Ref.4. Source: TAIR endosome Inferred from direct assay PubMed 22923678. Source: TAIR integral to 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_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 998

998

Calcium-transporting ATPase 3, endoplasmic reticulum-type

PRO_0000046407

Regions

Topological domain

1 – 48

Cytoplasmic Potential

Transmembrane

49 – 69

Helical; Potential

Topological domain

70 – 89

Lumenal Potential

Transmembrane

90 – 109

Helical; Potential

Topological domain

110 – 250

141

Cytoplasmic Potential

Transmembrane

251 – 270

Helical; Potential

Topological domain

271 – 291

Lumenal Potential

Transmembrane

292 – 309

Helical; Potential

Topological domain

310 – 746

437

Cytoplasmic Potential

Transmembrane

747 – 766

Helical; Potential

Topological domain

767 – 776

Lumenal Potential

Transmembrane

777 – 797

Helical; Potential

Topological domain

798 – 817

Cytoplasmic Potential

Transmembrane

818 – 840

Helical; Potential

Topological domain

841 – 883

Lumenal Potential

Transmembrane

884 – 903

Helical; Potential

Topological domain

904 – 916

Cytoplasmic Potential

Transmembrane

917 – 935

Helical; Potential

Topological domain

936 – 950

Lumenal Potential

Transmembrane

951 – 971

Helical; Potential

Topological domain

972 – 998

Cytoplasmic Potential

Sites

Active site

347

4-aspartylphosphate intermediate By similarity

Metal binding

300

Calcium 2; via carbonyl oxygen By similarity

Metal binding

301

Calcium 2; via carbonyl oxygen By similarity

Metal binding

303

Calcium 2; via carbonyl oxygen By similarity

Metal binding

305

Calcium 2 By similarity

Metal binding

692

Magnesium By similarity

Metal binding

696

Magnesium By similarity

Metal binding

757

Calcium 1 By similarity

Metal binding

760

Calcium 1 By similarity

Metal binding

785

Calcium 2 By similarity

Metal binding

788

Calcium 1 By similarity

Metal binding

789

Calcium 1 By similarity

Metal binding

789

Calcium 2 By similarity

Metal binding

894

Calcium 1 By similarity

Experimental info

Sequence conflict

R → G in CAA10660. Ref.2

Sequence conflict

55 – 56

KQ → NS in AAD29961. Ref.1

Sequence conflict

200

D → N in AAT68271. Ref.4

Sequence conflict

378 – 381

TVSG → LLVE in AAD29961. Ref.1

Sequence conflict

411

A → T in AAT68271. Ref.4

Sequence conflict

549

S → R in CAA10660. Ref.2

Sequence conflict

586

Missing in AAT68271. Ref.4

Sequence conflict

747

K → R in AAD29961. Ref.1

Sequence conflict

943 – 944

FS → CA in AAD29961. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SY55 [UniParc].

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

FASTA

998

109,060

        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' referencesShow '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. 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. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

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.
IPI	IPI00544163.
PIR	T00633. T52581.
RefSeq	NP_563860.1. NM_100887.2.
UniGene	At.24768.
3D structure databases
ProteinModelPortal	Q9SY55.
SMR	Q9SY55. Positions 1-976.
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.2.19. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PaxDb	Q9SY55.
PRIDE	Q9SY55.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G10130.1; AT1G10130.1; AT1G10130.
GeneID	837550.
KEGG	ath:AT1G10130.
Organism-specific databases
TAIR	At1g10130.
Phylogenomic databases
eggNOG	COG0474.
HOGENOM	HOG000265621.
InParanoid	Q9SY55.
KO	K01537.
OMA	MSTINDF.
PhylomeDB	Q9SY55.
ProtClustDB	CLSN2687751.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14610.
Gene expression databases
ArrayExpress	Q9SY55.
Genevestigator	Q9SY55.
GermOnline	AT1G10130. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR005782. 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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
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	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECA3_ARATH

Accession

Primary (citable) accession number: Q9SY55
Secondary accession number(s): Q0WP80

Q9SWS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents