ID A0A0V0UFT6_9BILA Unreviewed; 1460 AA.
AC A0A0V0UFT6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2B3 {ECO:0000313|EMBL:KRX49639.1};
GN ORFNames=T05_14132 {ECO:0000313|EMBL:KRX49639.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX49639.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX49639.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX49639.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX49639.1}.
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DR EMBL; JYDJ01000014; KRX49639.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0UFT6; -.
DR Proteomes; UP000055048; 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; 3.
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; 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: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:UP000055048};
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 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 466..489
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 509..538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 958..977
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 989..1010
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1031..1052
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1072..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1111..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 130..201
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 365..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 162459 MW; 40D554F599C0BFA6 CRC64;
MNQPNCKSSL IGNDVRQGGL RVYCGRAAFA HGLSWHRGTG QDCPRLWRHE GVVPQVENFT
YTWYVRCAFG VAFEIAMGLC EKWVFVLFLC FLLLLSLSSL FTLCNEQAAD ERATHHRSIV
EMNKSIRFPA YFALIFRLLL ALLAWGLSDP SDIERRRQIF GANYIPPQKP KAFFQLVWEA
LQDITLIILV AAAIISLGLS FYSPPHDSEF GGDDSEQQAS WIEGLAILVS VVVVVLVTAG
NDYTKERQFR GLQQKIEHEH KFSVIRNGEQ TQIFVTDLVV GDICMVKYGD LIPTDGIIIQ
SNDLKVDESS LTGESDFIKK SVDTDPFLLS GTHVMEGSGK VVVTAVGLNS QTGIIMTLLG
AAKSVEEEEM KKRKKQGRKK NRKNKSFSVE PHDATQSLLA GTDLHNSKVP GDGVVISDGE
THLHAAANLK PDKKRDEQQQ QQQQQQSQQS YTKKERSVLQ AKLTRLAIQI GYGGSFIAAL
TVIILILRFC IEEYGIKARP ISVLDVQYFV KFIIIGVTVL VVAVPEGLPL AVTLALAYSV
KKMMKDNNLV RHLDACETMG NATAICSDKT GTLTTNRMTV VRSYIGKSLY KEIPKWDQLD
ENIRSLMLTC ISVNSSYASQ VVPGEKGQLP KQLGNKTECG LLGFVMAMGQ SYQRVRDEVP
EDRLVKVYTF NSVRKSMSTV IEKNDSQGGY RLFSKGASEI LLGKCKFILG ADGTAQVFRQ
QDKDEMVRRV IEPMACDGLR TICLAYKDFV AANPENNQMQ YRGQIDWDDE NAVVKDLTCI
AIVGIQDPVR PEVPDAIRKC QRAGITVRMV TGDNVNTARS IAMQCGIIEP GSDFLILEGR
EFNARIRDQN GEIRQELLDQ VWPRLRVLAR SSPTDKYTLV KGMIDSSYSA NREVVAVTGD
GTNDGPALKK ADVGFAMGIA GTDVAKEASD IILTDDNFTS IVKAVMWGRN VYDSIAKFLQ
FQLTVNVVAV VVAFIGACAI EDSPLKAVQM LWVNLIMDTF AALALATEVP TEELLRRKPY
GRTKALISRT MMKNIIGHSL YQLVVIFTLV FVGERIFDID NGRYAKLHAP PTQHFTIVFN
TFVMLTLFNE INARKIHGQR NIFEGLLRNP IYYCILGGTF ICQIFIVQFG GFFFSTAALT
ADQWLWCIFL GLGDLLWGQV VTSIPSKKLP KKLTAFSEGT EIPIIFENPK GEGDEDDMDN
RSGQILWLRG LTRLQTQLRV VKAFKSTMED LDDQRSMVSG QSCLSLRSLR SHSYRPFYEF
RCNNPYENFS RNSFTSLREA RTFGDSKFLL SDIPEVVDAQ ASCGYKITNM NMILKPPKDG
IGKSASFDLR SGYVRHVIGG QLTEHLIPVP LSKTPTDQAI RVVNAFRMGM ERREPSLCGP
SVQRLREISR QLQLQQAQER SHRASTLLSS MPASLMAGGN RSSPSSPTSD PSTDMPSVRI
KPASARNSEA THPKTSTSAV
//