ID A0A0V1A9P6_9BILA Unreviewed; 1467 AA.
AC A0A0V1A9P6;
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:KRY21230.1};
GN ORFNames=T12_11432 {ECO:0000313|EMBL:KRY21230.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY21230.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY21230.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY21230.1};
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:KRY21230.1}.
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DR EMBL; JYDQ01000018; KRY21230.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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; 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 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:UP000054783};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1467
FT /note="Calcium-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006874380"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 413..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 456..485
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 905..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 936..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 978..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1019..1038
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1058..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 82..148
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 312..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 162725 MW; A5E52C5436EBA2EF CRC64;
MLSFVLLYIL SEVSLLRDCK SSLIGNDVRQ GGLRVYCGRA AFAHGLSWHR GTGQDCPRLW
RHEGVVPQVE NFTYTWYVRC AFGVAFEIAM GLCLSDPSDI ERRRQIFGAN YIPPQKPKAF
FQLVWEALQD ITLIILVAAA IISLGLSFYS PPHDSEFGGD DSEQQASWIE GLAILVSVVV
VVLVTAGNDY TKERQFRGLQ QKIEHEHKFS VIRNGEQTQI FVTDLVVGDI CMVKYGDLIP
TDGIIIQSND LKVDESSLTG ESDFIKKSVD TDPFLLSGTH VMEGSGKVVV TAVGLNSQTG
IIMTLLGAAK SVEEEEMKKR KKQGRKKNRK NKSFSVEPHD ATQSLLAGTD LHNSKVPGDG
VVISDGETHL HAAANLKPDK KRDEQQQQQQ QQQSQQSYTK KERSVLQAKL TRLAIQIGYG
GSFIAALTVI ILILRFCIEE YGIKARPISV LDVQYFVKFI IIGVTVLVVA VPEGLPLAVT
LALAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TTNRMTVVRS YIGKSLYKEI
PKWDQLDENI RSLMLTCISV NSSYASQVVP GEKGQLPKQL GNKTECGLLG FVMAMGQSYQ
RVRDEVPEDR LVKVYTFNSV RKSMSTVIEK NDSQGGYRLF SKGASEILLG KCKFILGADG
TAQVFRQQDK DEMVRRVIEP MACDGLRTIC LAYKDFVAAN PENNQIQYRG QIDWDDENAV
VKDLTCIAIV GIQDPVRPEV PDAIRKCQRA GITVRMVTGD NVNTARSIAM QCGIIEPGSD
FLILEGREFN ARIRDQNGEI RQELLDQVWP RLRVLARSSP TDKYTLVKGM IDSSYSANRE
VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK AVMWGRNVYD
SIAKFLQFQL TVNVVAVVVA FIGACAIEDS PLKAVQMLWV NLIMDTFAAL ALATEVPTEE
LLRRKPYGRT KALISRTMMK NIIGHSLYQL VVIFTLVFVG ERIFDIDNGR YAKLHAPPTQ
HFTIVFNTFV MLTLFNEINA RKIHGQRNIF EGLLRNPIYY CILGGTFICQ IFIVQFGGFF
FSTAALTADQ WLWCIFLGLG DLLWGQVVTS IPSKKLPKKL TAFSEGTEIP IIFENPKGEG
DEDDMDNRSG QILWLRGLTR LQTQCSTVTA RYSTPIALLT LSDDDGNDLV RVTMPTSMHG
MLVALFAAVF AKLNRCGQSL RCSLLRVVKA FKSTMEDLDD QRSMVSGQSC LSLRSLRSHS
YRPFYEFRCN NPYENFSRNS FTSLREARTF GDSKFLLSDI PEVVDAQASC GYKITNMNMI
LKPPKDGIGK SASFDLRSGY VRHVIGGQLT EHLIPVPLSK TPTDQAIRVV NAFRMGMERR
EPSLCGPSVQ RLREISRQLQ LQQAQERSHR ASTLLSSMPA SLMAGGNRSS PSSPTSDPST
DMPSVRIKPA SARNSETTHP KTSTSAV
//