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Database: UniProt
Entry: D7MSC1_ARALL
LinkDB: D7MSC1_ARALL
Original site: D7MSC1_ARALL 
ID   D7MSC1_ARALL            Unreviewed;       839 AA.
AC   D7MSC1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ARALYDRAFT_918363 {ECO:0000313|EMBL:EFH42207.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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DR   EMBL; GL348720; EFH42207.1; -; Genomic_DNA.
DR   RefSeq; XP_002865948.1; XM_002865902.1.
DR   AlphaFoldDB; D7MSC1; -.
DR   STRING; 81972.D7MSC1; -.
DR   EnsemblPlants; scaffold_801763.1; scaffold_801763.1; scaffold_801763.1.
DR   Gramene; scaffold_801763.1; scaffold_801763.1; scaffold_801763.1.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
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; 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   PANTHER; PTHR24093:SF514; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
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.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        170..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        665..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        780..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        813..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   DOMAIN          659..823
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
SQ   SEQUENCE   839 AA;  92984 MW;  C46FA5B1BBF8258D CRC64;
     MMITQKQNQQ TVIGLSNLLK TNLKVGIDDD DDEILHRRQT FGSNTYPCKK GKSLSRFIWK
     ASQFPPSLLI TLAAVIQSLL RIRRKVTRGG GSVWVSIYDI VVGDIVPLRN GGQVQKDLQI
     DPFLLSGSKL IEGIGTMLVT SVGMNTEWGQ MMEIAHDTDE EKPFQVYLKW IANSASCLVV
     LFALVACIVQ LCRYFYGRTK TSDGNPMFIL GITTAKEATE FVIKSLSFGI ATIIVGVPVG
     LPIAVLLKQV LSFICNQLFP ASLDLPEYQF KHLFSAKQMS VVDVWAGEIR MQDMDNGSQL
     PTLLKELIIE GIAQNTNGSV VLETGVSPTE QAILSFGNKL GMKFDDVRSA SLGRHTIPFN
     PDKKYGGVAL KLSTRALVHW KGSAKIILNS CEKYMDGSDN PIAIDEQKRK GFEETIKYMC
     ERGLRCAALA YQPYELEKLP SNEALSRLPS LPGKLVLLAI IGIEDPCRPG TKEEIQLCQS
     GGVKVRMVTD DDILTATAIA KKCGIFDEAS DGNILTGAEF RNLSDLEREE RVEDLLVLAE
     SSPSENLLFV KALKKRQHVV AATGMGIHDS ETLMAADVGL AMGIGGTAAA KEKSDIIILD
     GEFATIIKED TKSLFWIMQV ILWCRYLYTN IQRCVLFRLT VSVSVVAICV AEVVIHNAFP
     LNTVQLLLLN LTIDIFGALA LAYRPPAHHL MGKPPVNIRD PLINTTMWNK LVIQVIHQVL
     SLALVHSEKI LELKHGPTGN AVKVMNTLIF NSFVFCMAFN NDFEIRSLDQ TFKEIFRENM
     FLVTITSTII FQIFVLKLLG LFNSSVKLDL KEWLVASVLG LLSQLATHFP LQAHQYNRN
//
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