ID A0A340XW84_LIPVE Unreviewed; 1463 AA.
AC A0A340XW84;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10B {ECO:0000313|RefSeq:XP_007464462.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007464462.1};
RN [1] {ECO:0000313|RefSeq:XP_007464462.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 RefSeq; XP_007464462.1; XM_007464400.1.
DR STRING; 118797.A0A340XW84; -.
DR GeneID; 103080240; -.
DR KEGG; lve:103080240; -.
DR CTD; 23120; -.
DR InParanoid; A0A340XW84; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000265300; Unplaced.
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; 2.
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; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF79; PHOSPHOLIPID-TRANSPORTING ATPASE VB; 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 SFLD; SFLDS00003; Haloacid_Dehalogenase; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 358..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1111..1130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1142..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1190..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1220..1239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1251..1270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1295..1314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 63..118
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1079..1321
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 489..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1463 AA; 164681 MW; FE6B593DDFC7BBE9 CRC64;
MALSVDSSWY RWQWRVRDGL PQSPSEATPL LSPEEGAQNY NLAQQRVVFP NNNVFHQDWA
KVSRRYSGNR ICTTKYTLFT FLPQNLLEQF HRWANLYFLF LVILNWMPSM EVFHREITML
PLAIVLFITM VKDGIEDFKR HRLDREINCS NIQIYERKEQ SYTQKCWKDV QVGDFIQMQC
NEIIPADILL LFSSDPSGIC HLETSNLDGE TNLKQRRVVK GFTQQEVQFQ PEGFHNIVVC
EKPNDHLNRF KGYMEHPDQS RTGFGSESLL LRGCTIRNTR VAVGIVIYAG HETKAMLNNS
GPRYKRSKIE RRMNTDIFFC IGILFLMCLT GAVGHSLWNG TFAEHPPFDV PDAEGNFLPL
ALGGFYMFLT MIILLQILIP ISLYVSIELV KLGQVFFLHN DLDLYDEETY LSIQCRALNI
TEDLGQIQYI FSDKTGTLTE NKMVFRRCTI MGHEYSHQEN AKRLETPEEL DSDSEEWTQY
RCLSFPARRD QGPATIRGQG GSQPLRSQSA RARIQGHWRQ RSRGRCEISQ PPVAFSSSIE
KDVTPDKNLL TKVRDAALWL ETLSHSRPAK PSLSTTSSTA DFFLALTICN SVTVSTTAEP
RQRVTVPPST KALVTSLEKI QQLFHRLKLS SLSQSFSTTA LSDVDLGESL GANMPTTDSE
ERDDASVSSG GYSTDGGYRS STGEQGDILG AGPGASLEEV LQAPALSLAG PEVCYEAESP
DEAALVHAAR AYSFTLVSRT PKQVTVRLPQ GTCLTFDVLC TLEFDSVRKR MSVVVRHPLT
GEIIVYTKGA DCVIMDLLED PACATDADVE KKVRKIRAQT QRHLDLYARD GLRTLCIAKK
ILSEEDFQRW ASSRHEAEAS LNNRDELLME TAQHLENQLT LLGATGVEDR LQEGVPDTVA
ALQEAGIRLW VLTGDKQQTA VNIAYACRLL DQKDTVYSIN TESQETCESI LSLVLEEVKQ
LHGPQKPDHK LSGFCLPSVT PPPTSGAAVP EVGLVIDGKT LNAIFQGKLE EKFLELTRYC
RSVLCCRSTP LQKSMLVKLV RDRLRAMTLS IGDGANDVSM IQAADIGIGI SGQEGMQAVM
SSDFAISHFR HLKKLLLVHG HWCYSRLARM VAYYFYKNVG YVNLLFWYQF FCGFSGSTMI
DYWQLIFFNL FFTSLPPLVF GVLDKDISME TLLALPELYK SGQNSECYNL LTFWISMADA
FYQSLVCFFI PYLTYKDSDI DVFTFGTPIN TVSLATILLH QAMEMKTWTI IHGLVLAGSF
LMYFVVSLVY NATCVTCNSP INPYWVMEGQ LSDPTFYLVC LLTPVVALLP RYFLLALQGT
YGKSLILKAQ KIDKLPMDKR ELEIQSWRSR QRTATVPGEA QPTHHPGPPA PEPSYRASXP
KSSSPVECKY KEDWVLPGER SSGDHIRDDP CSWDSWAKFS SGEHLLLEPS RMMASGAYSS
GQTNSNRPFS QGSHRRSQSS VTI
//
