ID A0A341BUP5_NEOAA Unreviewed; 1464 AA.
AC A0A341BUP5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_024606376.1};
OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS (Neophocaena phocaenoides subsp. asiaeorientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Neophocaena.
OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024606376.1};
RN [1] {ECO:0000313|RefSeq:XP_024606376.1}
RP IDENTIFICATION.
RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024606376.1};
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_024606376.1; XM_024750608.1.
DR STRING; 1706337.A0A341BUP5; -.
DR KEGG; nasi:112403235; -.
DR InParanoid; A0A341BUP5; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000252040; 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:UP000252040};
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 1112..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1143..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1191..1215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1221..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1296..1315
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 1080..1322
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 637..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 164692 MW; 07767FCDE62761EE CRC64;
MALSVDSSRY RWQWRVRDGL PQSPSEATPL LSPEEGAQNY NLAQQRVVFP NNDVFHQDWA
KVSRRYSGNR ICTTKYTLFT FLPQNLLEQF HRWANLYFLF LVILNWMPSM EVFHREITML
PLAIVLFITM VKDGIEDFKR HRLDREINCS NIQIYERKEQ SYTQKCWKDV QVGDFIQMQC
NEIIPADILL LFSSDPSGIC HLETSNLDGE TNLKQRCVVK GFTQQEVQFR PEGFHNIIVC
EKPSNHLNRF KGYMEHLDRS RTGFGSESLL LQGCTIRNTK VAVGIVIYAG HETKAMLNNS
GPRYKRSKIE RRMNTDIFFC IGILFLMCLT GAVGHSLWNG TFAEHPPFDV PDAEGNFLPL
ALGGFYTFLT MIILLQILIP ISLYVSIELV KLGQVFFLHN DLDLYDEETH LSIQCRALNI
TEDLGQIQYI FSDKTGTLTE NKMVFRRCTI MGHEYSHQEN AKRLETPEEL DSDSEEWTQY
RCLSFPARRD QGPATIRGQG GSQPLRSQSA RARIQGHWRQ RSGGRCEISQ PPVAFSSSIE
KDVTPDKNLL TKVRDAALWL ETLSASRPAK PSLSTTSSTA DFFLALTICN SVTVSTTAEP
RQRVTVPPST KALVTSLEKI QQLFRRLKLS SLSQSFSTTA PSDVDLGERL GANMPTTDSE
ERDDVSVSSG GYSTDGGSRS STWEQGDILG VGPGASLEEV LQDPALGLAG PEVCYEAESP
DEAALVHAAR AYSFTLVSRT PKQVTVRLPQ GACLTFDVLC TLEFDSVRKR MSVVVRHPLT
GEIIVYTKGA DCVIMDLLED PACATDPDVE KKVRKIRAQT QRHLDLYARD GLRTLCIAKK
ILSEEDFQRW ASFRREAEAS LNNRDELLVE TAQHLENQLI LLGATGIEDR LQEGVPDTVA
ALQEAGIRLW VLTGDKQQTA VNIAYACRLL DQKDTVYSIN TESQETCESI LNLVLEEVKQ
LHGPQKPDHK LPGFFRLPSA TPPPTSGAAV PEVGLVIDGK TLNAIFQGKL EEKFLELTQY
CRSVLCCRST PLQKSMLVKL ARDRLRAMTL SIGDGANDVS MIQAADIGIG ISGQEGMQAV
MSSDFAISHF RHLKKLLLVH GHWCYSRLAR MVAYYFYKNV GYVNLLFWYQ FFCGFSGSTM
IDYWQLIFFN LFFTSLPPLV FGVLDKDVSM ETLLALPELY KSGQNSECYN LLTFWISMAD
AFYQSLVCFF IPYLTYKDSD IDVFTFGTPI NTVSLATILL HQAMEMKTWT IIHGLVLAGS
FLMYFVVSLL YNATCVTCNS PINPYWVMEG QLSDPTFYLV CLLTPVVALL PRYFLLALQG
TYGKSLILKA QKIDKLPMDK RELEIQSWRS RQRPATVPGE AQPTHRPGPP APEPSFRAST
PKSSSPVECK YKEDWVLPGE RSSGDHIRDD PCSRDSRAKL SSGEHLLLEP SRMMASGAYS
SGQTNSNRPF SQGSHRRSQS SVTI
//
