ID A0A4E0RV13_FASHE Unreviewed; 1164 AA.
AC A0A4E0RV13;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=D915_003311 {ECO:0000313|EMBL:THD26018.1};
OS Fasciola hepatica (Liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=6192 {ECO:0000313|EMBL:THD26018.1, ECO:0000313|Proteomes:UP000230066};
RN [1] {ECO:0000313|EMBL:THD26018.1, ECO:0000313|Proteomes:UP000230066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Choi Y.-J., Martin J., Mitreva M.;
RT "Improved annotation for the trematode Fasciola hepatica.";
RL Submitted (MAR-2019) 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|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. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THD26018.1}.
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DR EMBL; JXXN02000899; THD26018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4E0RV13; -.
DR Proteomes; UP000230066; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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 CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
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; 3.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW 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:UP000230066};
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 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 351..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 395..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 844..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 925..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 995..1016
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1028..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 42..114
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 279..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1087
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 128269 MW; C853BA6A0D641B9C CRC64;
MEPTERTPLA SAAPGSFDVE LDDLRRLMGN RKEEVSKYLQ EKFGGLSGLC KRLKTSPTNG
LMEDDFTKRK EKYGVNVIAQ QKSKTFCELV GEALQDLTLI VLIVAAVISL ALSLYIKYGQ
AATFDESEGQ AGWIEGLAIL IAVVVVVLVV ALNDYQKEKQ FRGLQSKIES EHTFFVIRKG
ETKQIPVQEI LVGDICQVKY GDLLPADGII IQCNDLKVDE SSLTGESDQV RKGEHKDPLL
LSGTHVMEGS GKMIVTAVGP NSQVGIIFGL LSSPQGEEAV AKSGKSNKKQ KKTEINNAKK
GGKNSGVIDG SVPDDNPKVA VVDQDKKKKK KTRRKEQSVL QAKLTKLAIQ IGYAGTCVAV
ATVLILIIKF AVITFAQNKE PWQTGKHLKQ IVNYVITGVT VLVVAVPEGL PLAVTLSLAY
SVKRMMKDNN LVRHLDACET MGNATAICSD KTGTLTTNRM TAVQCYIGDQ HYRNIPDQSQ
LPQPIMDLLV RGIAINSGYT SKILPPDTVG GLPKQVGNKT ECALLGFVQS LGRNYEVIRE
QWPEDKLYKV YTFNSVRKSM STVIKESENP KCFLLFTKGA SEMVVKHCSW FLDAHGNPRA
FGPSDQENLT VSVIEPMASE GLRTICVAYK RIIVGGSSNL PNDMVLREEP NWDDEEHLLT
GLTGLAIVAI EDPVRPEVPA AIRQCQRAGI TVRMVTGDNV NTARSIAIKC GILQPGENFL
VLEGQEFNKR IRDKVTGKVI QALFDKVWIN LRVLARSSPQ DKYILVSHII RSRAGSSRQV
VAVTGDGTND GPALKRADVG FAMGIAGTDV AKEASDIILT DDNFSSIVKA VMWGRNVYDS
ITKFLQFQLT VNVVAIIVAF AGACFLDDSP LKAIQMLWVN LIMDTLASLA LATEQPSPEL
LERAPYGRTQ PLISRQMAKN ILGHSVYQLG VIFFLLTGAH LFIEVDNMTG VRIHEPTQHF
TLIFNTLVLM TLFNEFNARK IHGQRNVFSG LQRNWLFVVI WFVTFVLQVL LIQFGSYAFS
TAPLTTDQWM WCLFFGVGEL IWGQVINTVP NAIIPICKCR KRAGAADAAG QEEEEEEEEE
EEEEEHEVDT VGRLPAAADL NLGGKILWVR GVNRIQTQMK VVDAFRMGLG PRIDPEQRRS
ISSLVLRHSQ NANIEYADAD APDV
//
