ECAP_SOLLC
ID ECAP_SOLLC Reviewed; 1048 AA.
AC Q42883;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Calcium-transporting ATPase, endoplasmic reticulum-type;
DE EC=7.2.2.10;
GN Name=LCA1 {ECO:0000312|EMBL:AAA34138.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA34138.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=1384045; DOI=10.1073/pnas.89.19.9205;
RA Wimmers L.E., Ewing N.N., Bennett A.B.;
RT "Higher plant Ca2+-ATPase: primary structure and regulation of mRNA
RT abundance by salt.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9205-9209(1992).
RN [2] {ECO:0000312|EMBL:AAD11617.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ohio state 4 {ECO:0000269|PubMed:10394952};
RC TISSUE=Root {ECO:0000269|PubMed:10394952};
RX PubMed=10394952; DOI=10.1023/a:1026410414091;
RA Navarro-Avino J.P., Hentzen A.E., Bennett A.B.;
RT "Alternative transcription initiation sites generate two LCA1 Ca2+-ATPase
RT mRNA transcripts in tomato roots.";
RL Plant Mol. Biol. 40:133-140(1999).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol to an
CC endomembrane compartment. {ECO:0000303|PubMed:1384045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: 9-fold higher level in roots compared with leaves.
CC {ECO:0000269|PubMed:1384045}.
CC -!- INDUCTION: 3-fold in leaves and 2-fold in roots 1 day after exposure to
CC high sodium chloride. {ECO:0000269|PubMed:1384045}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; M96324; AAA34138.1; -; Genomic_DNA.
DR EMBL; AF050495; AAD11617.1; -; mRNA.
DR EMBL; AF050496; AAD11618.1; -; mRNA.
DR PIR; A46284; S27763.
DR RefSeq; NP_001234073.1; NM_001247144.2.
DR RefSeq; XP_010323817.1; XM_010325515.2.
DR RefSeq; XP_010323824.1; XM_010325522.2.
DR RefSeq; XP_010323830.1; XM_010325528.2.
DR AlphaFoldDB; Q42883; -.
DR SMR; Q42883; -.
DR STRING; 4081.Solyc01g096190.2.1; -.
DR PaxDb; Q42883; -.
DR PRIDE; Q42883; -.
DR EnsemblPlants; Solyc01g096190.3.1; Solyc01g096190.3.1; Solyc01g096190.3.
DR GeneID; 543554; -.
DR Gramene; Solyc01g096190.3.1; Solyc01g096190.3.1; Solyc01g096190.3.
DR KEGG; sly:543554; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; Q42883; -.
DR OMA; FISWDVV; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q42883; -.
DR BioCyc; MetaCyc:MON-14597; -.
DR BRENDA; 7.2.2.10; 3101.
DR Proteomes; UP000004994; Chromosome 1.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISS:UniProtKB.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Calcium transport; Endoplasmic reticulum;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1048
FT /note="Calcium-transporting ATPase, endoplasmic reticulum-
FT type"
FT /id="PRO_0000046409"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..93
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..267
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..800
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..883
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..944
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..965
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 966..981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1007
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 366
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 728
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 732
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 794
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 797
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 822
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 825
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 826
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 826
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 957
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
SQ SEQUENCE 1048 AA; 116128 MW; D029CEE2A8E1A294 CRC64;
MEEKPFPAWS WSVDQCLKEY QVKLEKGLST YEVDKRRERY GLNELEKEKG KPLWRLVLEQ
FDDTLVKILL GAAFISFVLA YVNQDETGES GFEAYVEPLV ILWILVLNAI VGVWQESNAE
KALEALKEMQ GESAKVLRDG YLVPDFPAKE LVPGDIVELR VGDKVPADMR VATLKSSTLR
VEQSSLTGES MPVTKSTDFL ATDDCELQAK ENMVFAGTTV VNGSCICIVV NTGMCTEIGK
IQRQIHDASM EESDTPLKKK LDEFGNRLTF AIGVVCLVVW AINYKYFLSW EVVDDWPSDF
RFSFEKCAYY FKIAVALAVA AIPEGLPSVI TTCLALGTRK MAQKNAIVRK LQSVETLGCT
TVICSDKTGT LTTNQMSVSE FFTLGRKTTA CRVFGVEGTT YDPKDGGIMN WNCCKMDANL
LLMAEICAIC NDAGVFCDGR LFKATGLPTE AALKVLVEKM GVPDSKARCK IRDAQIVSSY
LIDRNTVKLG CCDWWMKRSK RVATLEFDRV RKSMGVIVRE PNGSNRLLVK GAFESLLERS
TYVQLADGST VPLDESCRQL LLLKQLEMSS KGLRCLGLAY KDDLGELSGY YAATHPAHKK
LLDPSCYSSI ESDLVFVGVV GLRDPPREEV HRAVNDCRRA GIKIMVITGD NKSTAEAVCR
EIQLFSNGEN LRGSSFTGKE FMAFSSQQQI EILSQDGGKV FSRAEPRHKQ EIVRMLKEMG
EIVAMTGDGV NDAPALKLAD IGIAMGITGT EVAKEASDMV LADDNFSTIV SAVAEGRSIY
NNMKAFIRYM ISSNVGEVIS IFLTAVLGIP ECLIPVQLLW VNLVTDGPPA TALGFNPADV
DIMQKPPRKN TDALINSWVF FRYMVIGSYV GIATVGIFIV WYTQASFLGI NIVSDGHTLV
ELSQLRNWGE CSTWTNFTVS PFKAGNRLIT FSDPCEYFTV GKVKAMTLSL SVLVAIEMFN
SLNALSEDNS LIKMPPWRNP WLLVAMSLSF ALHSVILYVP FLADIFGIVP LSLYEWLLVI
LLSAPVILID EVLKFVGRRR RRTKLKAA
