Calcium-transporting ATPase, endoplasmic reticulum-type

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Reviewed, UniProtKB/Swiss-Prot Q42883 (ECAP_SOLLC)

Last modified June 16, 2009. Version 58. History...

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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 names

Recommended name:
Calcium-transporting ATPase, endoplasmic reticulum-type
EC=3.6.3.8

Gene names

Name:

LCA1

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

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Protein attributes

Sequence length	1048 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 to an endomembrane compartment. Ref.1
Catalytic activity	ATP + H₂O + Ca²⁺(Cis) = ADP + phosphate + Ca²⁺(Trans). UniProtKB P92939
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Tissue specificity	9-fold higher level in roots compared with leaves. Ref.1
Induction	3-fold in leaves and 2-fold in roots 1 day after exposure to high sodium chloride. Ref.1
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

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Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro calcium ion transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1048

1048

Calcium-transporting ATPase, endoplasmic reticulum-type

PRO_0000046409

Regions

Topological domain

1 – 63

Cytoplasmic Potential

Transmembrane

64 – 84

1 Potential

Topological domain

85 – 93

Lumenal Potential

Transmembrane

94 – 114

2 Potential

Topological domain

115 – 213

Cytoplasmic Potential

Transmembrane

214 – 234

3 Potential

Topological domain

235 – 267

Lumenal Potential

Transmembrane

268 – 288

4 Potential

Topological domain

289 – 312

Cytoplasmic Potential

Transmembrane

313 – 333

5 Potential

Topological domain

334 – 800

467

Lumenal Potential

Transmembrane

801 – 821

6 Potential

Topological domain

822 – 862

Cytoplasmic Potential

Transmembrane

863 – 883

7 Potential

Topological domain

884 – 944

Lumenal Potential

Transmembrane

945 – 965

8 Potential

Topological domain

966 – 981

Cytoplasmic Potential

Transmembrane

982 – 1002

9 Potential

Topological domain

1003 – 1007

Lumenal Potential

Transmembrane

1008 – 1028

10 Potential

Topological domain

1029 – 1048

Cytoplasmic Potential

Compositional bias

1038 – 1042

Poly-Arg

Sites

Active site

366

4-aspartylphosphate intermediate By similarity UniProtKB P04191

Metal binding

319

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

320

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

322

Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191

Metal binding

324

Calcium 2 By similarity UniProtKB P04191

Metal binding

728

Magnesium By similarity UniProtKB P04191

Metal binding

732

Magnesium By similarity UniProtKB P04191

Metal binding

794

Calcium 1 By similarity UniProtKB P04191

Metal binding

797

Calcium 1 By similarity UniProtKB P04191

Metal binding

822

Calcium 2 By similarity UniProtKB P04191

Metal binding

825

Calcium 1 By similarity UniProtKB P04191

Metal binding

826

Calcium 1 By similarity UniProtKB P04191

Metal binding

826

Calcium 2 By similarity UniProtKB P04191

Metal binding

957

Calcium 1 By similarity UniProtKB P04191

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Sequences

Sequence

Length

Mass (Da)

Tools

Q42883-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D029CEE2A8E1A294
Show »

FASTA

1,048

116,128

        10         20         30         40         50         60 
MEEKPFPAWS WSVDQCLKEY QVKLEKGLST YEVDKRRERY GLNELEKEKG KPLWRLVLEQ 

        70         80         90        100        110        120 
FDDTLVKILL GAAFISFVLA YVNQDETGES GFEAYVEPLV ILWILVLNAI VGVWQESNAE 

       130        140        150        160        170        180 
KALEALKEMQ GESAKVLRDG YLVPDFPAKE LVPGDIVELR VGDKVPADMR VATLKSSTLR 

       190        200        210        220        230        240 
VEQSSLTGES MPVTKSTDFL ATDDCELQAK ENMVFAGTTV VNGSCICIVV NTGMCTEIGK 

       250        260        270        280        290        300 
IQRQIHDASM EESDTPLKKK LDEFGNRLTF AIGVVCLVVW AINYKYFLSW EVVDDWPSDF 

       310        320        330        340        350        360 
RFSFEKCAYY FKIAVALAVA AIPEGLPSVI TTCLALGTRK MAQKNAIVRK LQSVETLGCT 

       370        380        390        400        410        420 
TVICSDKTGT LTTNQMSVSE FFTLGRKTTA CRVFGVEGTT YDPKDGGIMN WNCCKMDANL 

       430        440        450        460        470        480 
LLMAEICAIC NDAGVFCDGR LFKATGLPTE AALKVLVEKM GVPDSKARCK IRDAQIVSSY 

       490        500        510        520        530        540 
LIDRNTVKLG CCDWWMKRSK RVATLEFDRV RKSMGVIVRE PNGSNRLLVK GAFESLLERS 

       550        560        570        580        590        600 
TYVQLADGST VPLDESCRQL LLLKQLEMSS KGLRCLGLAY KDDLGELSGY YAATHPAHKK 

       610        620        630        640        650        660 
LLDPSCYSSI ESDLVFVGVV GLRDPPREEV HRAVNDCRRA GIKIMVITGD NKSTAEAVCR 

       670        680        690        700        710        720 
EIQLFSNGEN LRGSSFTGKE FMAFSSQQQI EILSQDGGKV FSRAEPRHKQ EIVRMLKEMG 

       730        740        750        760        770        780 
EIVAMTGDGV NDAPALKLAD IGIAMGITGT EVAKEASDMV LADDNFSTIV SAVAEGRSIY 

       790        800        810        820        830        840 
NNMKAFIRYM ISSNVGEVIS IFLTAVLGIP ECLIPVQLLW VNLVTDGPPA TALGFNPADV 

       850        860        870        880        890        900 
DIMQKPPRKN TDALINSWVF FRYMVIGSYV GIATVGIFIV WYTQASFLGI NIVSDGHTLV 

       910        920        930        940        950        960 
ELSQLRNWGE CSTWTNFTVS PFKAGNRLIT FSDPCEYFTV GKVKAMTLSL SVLVAIEMFN 

       970        980        990       1000       1010       1020 
SLNALSEDNS LIKMPPWRNP WLLVAMSLSF ALHSVILYVP FLADIFGIVP LSLYEWLLVI 

      1030       1040 
LLSAPVILID EVLKFVGRRR RRTKLKAA

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References

[1]	"Higher plant Ca2+-ATPase: primary structure and regulation of mRNA abundance by salt." Wimmers L.E., Ewing N.N., Bennett A.B. Proc. Natl. Acad. Sci. U.S.A. 89:9205-9209(1992) [PubMed: 1384045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
[2]	"Alternative transcription initiation sites generate two LCA1 Ca2+-ATPase mRNA transcripts in tomato roots." Navarro-Avino J.P., Hentzen A.E., Bennett A.B. Plant Mol. Biol. 40:133-140(1999) [PubMed: 10394952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Ohio state 4. Tissue: Root.

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Cross-references

Sequence databases
	M96324 Genomic DNA. Translation: AAA34138.1. AF050495 mRNA. Translation: AAD11617.1. AF050496 mRNA. Translation: AAD11618.1.
PIR	S27763. A46284.
UniGene	Les.34
3D structure databases
HSSP	HSSP built from PDB template 1SU4 based on UniProtKB P04191.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.6.3.8. 281054.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 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.
TIGRFAMs	TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ECAP_SOLLC

Accession

Primary (citable) accession number: Q42883

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents