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Database: UniProt
Entry: A0A3B6LPF7_WHEAT
LinkDB: A0A3B6LPF7_WHEAT
Original site: A0A3B6LPF7_WHEAT 
ID   A0A3B6LPF7_WHEAT        Unreviewed;      1066 AA.
AC   A0A3B6LPF7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=CFC21_072336 {ECO:0000313|EMBL:KAF7066334.1};
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:TraesCS5B02G276500.2};
RN   [1] {ECO:0000313|EMBL:KAF7066334.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7066334.1};
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:TraesCS5B02G276500.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS5B02G276500.2};
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:TraesCS5B02G276500.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7066334.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7066334.1};
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}.
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DR   EMBL; CM022224; KAF7066334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6LPF7; -.
DR   EnsemblPlants; TraesCS5B02G276500.2; TraesCS5B02G276500.2; TraesCS5B02G276500.
DR   Gramene; TraesCS5B02G276500.2; TraesCS5B02G276500.2; TraesCS5B02G276500.
DR   Gramene; TraesCS5B03G0718200.2; TraesCS5B03G0718200.2.CDS; TraesCS5B03G0718200.
DR   OMA; HKHAHIN; -.
DR   Proteomes; UP000019116; Chromosome 5B.
DR   Proteomes; UP000815260; Chromosome 5B.
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; IEA:UniProtKB-EC.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
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; 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; 2.
DR   PANTHER; PTHR24093:SF436; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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   SMART; SM00831; Cation_ATPase_N; 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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        349..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        401..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        823..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        890..909
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        967..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        999..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          113..187
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1066 AA;  116728 MW;  52B4AB7BAAECFCBC CRC64;
     MWYFLLHVSS YIITYSMPFL PSFQQIALVL NASRRFRYTL DLARDEEREN LRRVIRAHAQ
     VIRAVFLFKK AGQKVLQESY NGAKFESLSQ TFPIDLEKLV MLNRDHDAIM LQEVGGVSGL
     SDLLKSNLDR GVSSNEDELL QRRDIFGANT YPRKKRKSIW RFVFEACQDL TLVILMVAAA
     ISLSLGMATE GVKDGWYDGG SIFFAVFLVI FVTATSDYRQ SLQFQHLNEE KQNIQVEVIR
     GGKRVGASIF DLVVGDVVPL KIGDQVPADG VLISGHSLAI DESTMTGESK IVHKDQNAPM
     LMSGCKVADG YGSMLVTGVG TNTEWGMLMA NLSEDIGEET PLQARLNGVA TLIGIVGLSV
     AGVVLVVLWI RYFTGHSNNP DGTTAFVAGT TGAKQGFMGA ISIFTIAVTI VVVAVPEGLP
     LAVTLTLAYS MRKMMRDKAL VRRLSSCETM GSATTICSDK TGTLTLNKMT VVEAYLSGTK
     LNPCHNTGMI SSSVASLLVE GIAQNTAGAV FSPEDGGAAE VAGSPTEKAI LSWGLKIGMN
     FNDVRSKSSV LRVLPFNSVK KCGGVAVQVS DAYVHIHWKG AAELVLASCK SWLSIDGSVH
     PMSFDKRSID DMAMSSLRCI AFAYCTCELT MVPREDLDKW QLPEDNLTLL GMVGIKDPCR
     PGVRDAVQLC SAAGVKVRMV TGDNVETAKA IAFECGILNS KDVASETIII EGKVFREMSE
     TAREEVAVKI TVMGRSSPND KLLLVQALKR KGHVVAVTGD GTNDAPALHE ADIGLSMGIS
     GTEVAKESSD IIILDDDFTS VVKVVRWGRS VYANIQKFIQ FQLTVNVAAL VINVVAAVSS
     GAVPLNAVEL LWVNLIMDTL GALALATEPP TDNLMKRHPV GRREPLVTNI MWRNLFIQAL
     YQIAVLLVFN FDGKRIFQLH NESREHADKI TNTFVFNAFV FCQIFNEFNA RKPEEKNVLR
     GVTSNRLFMG IVGITTILQI LIIEFLGKFF GTVRLVWKLW LLSVAIGAVS WPLAYVGKSI
     PVPARPFQDY LKHCCAWRRP RRRGNFPAYT AADPCVYFCF HPTSSS
//
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