ID A0A4S2KQ13_9HYME Unreviewed; 1374 AA.
AC A0A4S2KQ13;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=DBV15_07461 {ECO:0000313|EMBL:TGZ49968.1};
OS Temnothorax longispinosus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Temnothorax.
OX NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ49968.1, ECO:0000313|Proteomes:UP000310200};
RN [1] {ECO:0000313|EMBL:TGZ49968.1, ECO:0000313|Proteomes:UP000310200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:TGZ49968.1};
RX PubMed=30967075;
RA Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA Bornberg-Bauer E., Foitzik S.;
RT "Ant behaviour and brain gene expression of defending hosts depend on the
RT ecological success of the intruding social parasite.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004127}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {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:TGZ49968.1}.
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DR EMBL; QBLH01002061; TGZ49968.1; -; Genomic_DNA.
DR STRING; 300112.A0A4S2KQ13; -.
DR Proteomes; UP000310200; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR FunFam; 1.20.1110.10:FF:000002; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000013; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000147; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000007; Calcium-transporting ATPase; 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 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; IPR059000; ATPase_P-type_domA.
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; 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 Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000310200};
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 105..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 382..405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 425..454
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 873..894
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1036..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1105..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 47..122
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 298..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..310
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..347
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 150595 MW; 556F91427C06C67B CRC64;
MNLASANEGN RDIMATIDGR PAQYGITLKQ LRELMEFRGR EGVNKINGHG GVQEICKKLY
TSPNEGLSGS AADIQHRRDT FGSNMIPPKP PKTFLQLVWE ALQDVTLIIL EVAALVSLGL
SFYQPGEDEE RPASAAMDED EAKYGWIEGL AILISVIVVV IVTAFNDYSK ERQFRGLQSR
IEGEHKFSVI RQGEVKQISV SDIVVGDICQ VKYGDLLPAD GILIQSNDLK VDESSLTGES
DHVKKGESFD PMVLSGTHVM EGSGKMLVAA VGVNSQAGII FTLLGAAVDQ QEQEIKKMKK
EAKKQRKKKS LPGEESVEIT GNSHVTGGGG GGGGGGGGGG GGGGGGGVKH EGGENHHTAA
PVSAEGSGKK EKSVLQAKLT KLAIQIGYAG STIAVLTVVI LIIQFCVKTF VMEGKPWRNI
YVGDLVRHLI IGVTVLVVAV PEGLPLAVTL SLAYSVKKMM KDNNLVRHLD ACETMGNATA
ICSDKTGTLT TNRMTVVQSY ICEKMCKTTP NFSDIPSHVG EXIIQAISID SAYTSRVMDP
PEPTELPMQV GNKTECALLG FVLALGKKYQ TVRDDYPEET FTRVYTFNSV RKSMSTVVPR
KGGGFRLFTK GASEIIMKKC AFIYGREGHL ETFTRDMQDR LVKNVIEPMA CNGLRTISIA
YRDFVPGKAE INQVHIDNEP NWDDEDNLVN NLTCLCIVGI EDPVRAEVPE AIRKCQKAGI
TVRMVTGDNI NTARSIALKC GILKPNEDFL ILEGKEFNRR IRDSNGEVQQ HLLDKVWPKL
RVLARSSPTD KYTLVKGIID SKATESREVV AVTGDGTNDG PALKKADVGF AMGIAGTDVA
KEASDIILTD DNFSSIVKAV MWGRNVYDSI AKFLQFQLTV NVVAVIVAFI GACAVQDSPL
KAVQMLWVNL IMDTLASLAL ATELPTPDLL LRRPYGRTKP LISRTMMKNI LGQAFYQLGV
IFSLLFAGEY RSFPPFSFPR LLHLINPSRR TFIVQYCYRA EPNGLKLSRT AITGDLMLDI
DTGRGVAATG GGPTQHFTVI FNTFVMMTLF NEFNARKIHG QRNVFQGIFT NPIFYSIWVG
TCVSQVIIIQ YGKMAFSTRA LTLDQWLWCL FFGIGTLIWG QIVTTIPTRR IPKILSAFKS
TLEDLEERRS VHSLHSLHSM RSSRSHTGPR PLSDFTYIDE DPTNTTTTTA QNVAYKSSNR
SAEPMMSQDY ETNYRGPSRM QQSLNSPASP LLLTVTGPAN AYNHHYTITN TITDNRSPSS
NALNQPLSPN HMAPMSSNRD NTGNSLLLSS NNLVLPELTK LIRVVNAFRQ GLDTRYGEHS
STTLAEVLRK QSSLSKRLSQ TSSIEYADNI PDELTIPEID VERLSSHSHT ETAV
//
