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Database: UniProt
Entry: Q58CL2_DROME
LinkDB: Q58CL2_DROME
Original site: Q58CL2_DROME 
ID   Q58CL2_DROME            Unreviewed;      1034 AA.
AC   Q58CL2;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=CG32451 {ECO:0000313|EMBL:AAX51640.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAX51640.1};
RN   [1] {ECO:0000313|EMBL:AAX51640.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:AAX51640.1};
RA   Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA   Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL   Submitted (MAR-2005) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC         Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC         Evidence={ECO:0000256|ARBA:ARBA00024272};
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. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; BT021935; AAX51640.1; -; mRNA.
DR   AlphaFoldDB; Q58CL2; -.
DR   PeptideAtlas; Q58CL2; -.
DR   VEuPathDB; VectorBase:FBgn0052451; -.
DR   ExpressionAtlas; Q58CL2; baseline and differential.
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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR   CDD; cd02085; P-type_ATPase_SPCA; 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; IPR006413; P-type_ATPase_IIA_PMR1.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|RuleBase:RU361146};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU361146}.
FT   DOMAIN          140..214
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1034 AA;  113717 MW;  8D672CDE96FCB2FA CRC64;
     MKNHNKYVKL PQNLDLSFHS DLDLLPDTAA DIDVELDPAA DTDVAALSVN VPASLGLDED
     DDDEVIIAPG GGGLRLAPTA AEAVAAHRQH HQQHQQCKQL KNQLEQKQIL PKSKICGLGS
     DSIVETGLTL TPEMLLSTSE SSTHSASEVA GRLQVDVRTG LKWTEAKYRA KIIGHNELLL
     VAEDPTWKKY IEQFRNPLIL LLLGSALVSV IMKQFDDAVS ITIAILIVVT VAFIQEYRSE
     KSLEELKKLV PPECHCLREG RLDTFLAREL VPGDIVHLNV GDRVPADVRL FEAVDLSIDE
     SSFTGETEPA RKITDVLLNN TNVKDHSNMK NIAFMGTLVR CGNGKGIVVS TGERSEFGEV
     FKMMQAEEAP KTPLQKSMDI LGAQLSFYSF LIIGVIMLLG WLQGKPLSEM FNISVSLAVA
     AIPEGLPIVV TVTLALGVMR MAKRNSIVKK LPTVETLGCV NVICSDKTGT LTKNKMTATI
     IITSDGYMAD VTGAGYNDQG EIHIRHCNNV EMAKTNITNL LEIGAVCNNA YIQNGTLLGQ
     PTEGALVAVA MKNGMYATAE NYVRIQEYPF SSEQKMMAVK CIHKYNNNKE EIFFAKGALE
     TLLPQCTKYQ FGTQTVPLTK QNEAEFLAEA YEIGRKGLRV LALAKGRSMQ DLIYCGLVGI
     TDPPRPLVRE SIEMLMQSGV RVKMVTGDAQ GTALAIANLI GIDTIHHQTL SGQEMDQMNE
     HQLDKVANNV SVFYRVSPRH KLEIVKSLQR SGNIVGMTGD GVNDGVALKK ADIGIAMGKN
     GTDVCKEAAD MILVNDDFHT IIAAIEEGKG IFYNIRNFVR FQLSTSIAAL ALIALATLMD
     IANPLNAMQI LWINIIMDGP PAQSLGVEPV DHDVLKQQPR NVKQPMITKS VVVNVLLSAS
     IIVLGTLWVF QREMADGTLG KTKRDTTMTF TCFVFFDMFN ALSCRSQTKS VFTIGLTTNR
     MFLLAVAFSI IGQMLVVYFP PLQMVFQTEA LTPYDIFFLV SLTSSVLVVS EIKKWFERTM
     ERKMYSTRSE LDFV
//
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