ID A0A3B6EQC2_WHEAT Unreviewed; 1043 AA.
AC A0A3B6EQC2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=CFC21_038056 {ECO:0000313|EMBL:KAF7025905.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3A02G475500.1};
RN [1] {ECO:0000313|EMBL:KAF7025905.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7025905.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3A02G475500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3A02G475500.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3A02G475500.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7025905.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7025905.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
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 Evidence={ECO:0000256|ARBA:ARBA00000363,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM022217; KAF7025905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6EQC2; -.
DR SMR; A0A3B6EQC2; -.
DR STRING; 4565.A0A3B6EQC2; -.
DR EnsemblPlants; TraesCS3A02G475500.1; TraesCS3A02G475500.1; TraesCS3A02G475500.
DR Gramene; TraesCAD_scaffold_038001_01G000100.1; TraesCAD_scaffold_038001_01G000100.1; TraesCAD_scaffold_038001_01G000100.
DR Gramene; TraesCLE_scaffold_049587_01G000300.1; TraesCLE_scaffold_049587_01G000300.1; TraesCLE_scaffold_049587_01G000300.
DR Gramene; TraesCS3A02G475500.1; TraesCS3A02G475500.1; TraesCS3A02G475500.
DR Gramene; TraesCS3A03G1110400.1; TraesCS3A03G1110400.1.CDS; TraesCS3A03G1110400.
DR Gramene; TraesKAR3A01G0439350.1; cds.TraesKAR3A01G0439350.1; TraesKAR3A01G0439350.
DR Gramene; TraesPAR_scaffold_047442_01G000100.1; TraesPAR_scaffold_047442_01G000100.1; TraesPAR_scaffold_047442_01G000100.
DR Gramene; TraesROB_scaffold_133251_01G000100.1; TraesROB_scaffold_133251_01G000100.1; TraesROB_scaffold_133251_01G000100.
DR Gramene; TraesWEE_scaffold_054951_01G000300.1; TraesWEE_scaffold_054951_01G000300.1; TraesWEE_scaffold_054951_01G000300.
DR OMA; DAMMKRP; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000019116; Chromosome 3A.
DR Proteomes; UP000815260; Chromosome 3A.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR024750; Ca_ATPase_N_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093:SF502; CALCIUM-TRANSPORTING ATPASE 1, PLASMA MEMBRANE-TYPE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12515; CaATP_NAI; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 401..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 830..855
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 964..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 997..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 13..56
FT /note="Calcium-transporting P-type ATPase N-terminal
FT autoinhibitory"
FT /evidence="ECO:0000259|Pfam:PF12515"
FT DOMAIN 124..189
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 846..1017
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1023..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 112774 MW; 328F5BC5D0F2D8E1 CRC64;
MSYLRKKSID FLKTFDVPAK NPSEDAQRRW REAVGTLVKN RRRRFRMVPD LDKRSQAETQ
RRNIQEKLRV ALYVQKAALQ FIDAARRVEH PLSELARQSG FSISAEELAS LVRGHDTKSL
RLHKGVEGLA RKVNVSLADG VRSDDVGVRG EVYGANHYPE KAARTFWMYL WDASQDTTLM
LLAFCAVISV VIGIATEGWP GGMYDGLGIM LTISLVVTIT AASDYKQSLQ FRDLDREKKK
IEIQVTRDGF RQKVSIYDIV VGDIVHLSIG DQVPADGLFI DGYSFIVDES SLSGESEPVH
VSATNRFLLG GTKVQDGSAR MLVTAVGMRT EWGNLMETLS QGGEDETPLQ VKLNGVATII
GKIGLAFAVL TFTVLMARFL IGKAASPGGL VTWGMEDALS VLNFFAVAVT IIVVAVPEGL
PLAVTLSLAF AMKKLMQERA LVRHLSACET MGSASCICTD KTGTLTTNHM VVEKVWAAGG
ATTVSTAKGF EEFTSSALSE GFAKLLLEGV FQCSGSEVVR SKDGKTSVMG TPTESAILEF
GLGVEKNTCI EHAAAAKLKV EPFNSVKKTM AVVVASPSAG GRPRAFLKGA SEVVLRRCSN
VVVDRHGSIV ALTEKNYMKQ VAGAIDKFAC EALRTLCLAY QDVGGENEVP NDGYTLIAVF
GIKDPLRPGV REAVRTCHVA GINVRMVTGD NISTAKAIAR ECGILTPDGV AIEGPEFRQM
SPDQMRAIIP KIQVMARSLP LDKHTLVTNL RGMFNEVVAV TGDGTNDAPA LHEADIGLAM
GIAGTEVAKE NADVIIMDDN FSTIINVAKW GRSVYINIQK FVQFQLTVNV VALMVNFVSA
SFTGSAPLTI VQLLWVNLIM DTLGALALAT EPPSDDMMRR PPVGRGDNFI TKVMWRNIAG
QSIFQLVVLG VLLARGDSLL HMNGDKELLN TFVFNTFVFC QVFNEVNSRE MEKINVFSGM
FSSWVFSAVV GATVGFQVIL VELLGTFAGT VHLNGRLWLM SVLVGSVGLV IGAVLKCIPV
GSGDASSDRH DGYQPIPTGP SAV
//
