ID T1HNG8_RHOPR Unreviewed; 1189 AA.
AC T1HNG8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC005592-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC005592-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; ACPB03015037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HNG8; -.
DR STRING; 13249.T1HNG8; -.
DR EnsemblMetazoa; RPRC005592-RA; RPRC005592-PA; RPRC005592.
DR VEuPathDB; VectorBase:RPRC005592; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; T1HNG8; -.
DR OMA; PECIHKL; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 263..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 908..929
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 991..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1095..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 6..71
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 878..1124
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1189 AA; 135448 MW; 31835476B5F44DAB CRC64;
ETERRIKAND RQFNAQFKYA NNYIKTSKYS LVTFLPLNLF EQFQRLANFY FLCLMVLQMI
NVISSLTPIT TAVPLIGVLC LTAIKDAYDD YERHISDSQV NNRRAMVVHE GKLVEGKWSQ
VRVGDVIRME NDQFVAADVL LLTTSEPSGL CFIETAELDG ETNLKSRQCL LETAAMGQDD
SQIGKFDGEI ICEPPNNLLN KFDGTLIWND KRYSLDNDKI LLRGCILRNT DWCYGVVVFA
GKDTKLMQNS GKTKFKRTSI DKLLNFLIIG IVFFLISICL FCMVACGVWE TITGRYFQIY
LPWDKLVPSE PITGATIISL LVFFSYAIVL NTVVPISLYV SVEVIRLFQS FLINWDEKMY
CEKTGMPAKA RTTTLNEELG QIQYIFSDKT GTLTQNIMTF NKCSITGKVY GEIIDKRTGE
VLEVNEDTEK VDFSFNPDYE PSFNFYDKSL LDAVKSKKDP DVDIFFKILA LCHTVMPAEK
NGNLKYQAQS PDEAALVSAA RNFGFVFRER SPNSITIEVL RKREVHELLC ILDFNNIRKR
MSVILRHKGK LRLYCKGADN VIYERLKKEI TAESSRFAGD GLRTLCLAVR ELDENYFNQW
KARHHEAALS MDNRDEKLDA IYEEIENNLT LIGSCTAIED KLQDGVPQTI ANLSAAGMKI
WVLTGDKQET AINIGYSCHL LSDEMEVMIV DGHTIEEVTK QLAKCRDTLM LGGHPMAQHN
NNSHHPAISS KFLSPCLMVR QFTERLLCTD IRILYVCYLI FLPISEKNVF TNSCETDYKQ
DAEEDTSLLF ALVINGHSLV HVFHPQVEKI FLEVSTMCKS VICCRVTPLQ KAMVVELIKK
TKRAVTLAIG DGANDVSMIK AAHIGIGVSG LEGNQAMLAS DYSIGQFRFL ERLLLVHGRW
SYYRMCKFLR YFFYKNFAFT LCHFWYAFFC GFSAQTVFDP MFIAVYNLFY TSLPVLSIGI
FDQDVNDKNS IAYPQLYTPG HTNLLFNKQE FLRSALYGFY TSCVLFFIPY GTYKDGVSPK
GHVLSDTMFL GSVVATILVI VVTAQVALDT SYWTVFNHIT IWGSLAWYFI LDNFYNYVIG
GSYVGSMTTA MKEATFWFTT GLTVVILIVP VIAWRFFFVD VFPTLSDRVR LKQRLASIRS
RQSHDMLRTP SARKARRSIR SGYAFSHQEG FGRLITSGKI MRKLPKSDF
//
