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Database: UniProt
Entry: A0A0V0UFT6_9BILA
LinkDB: A0A0V0UFT6_9BILA
Original site: A0A0V0UFT6_9BILA 
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
//
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