ID A0A2Y9QEC0_DELLE Unreviewed; 1167 AA.
AC A0A2Y9QEC0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC111188071 {ECO:0000313|RefSeq:XP_022455971.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455971.1};
RN [1] {ECO:0000313|RefSeq:XP_022455971.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455971.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022455971.1; XM_022600263.2.
DR AlphaFoldDB; A0A2Y9QEC0; -.
DR STRING; 9749.A0A2Y9QEC0; -.
DR KEGG; dle:111188071; -.
DR InParanoid; A0A2Y9QEC0; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000248483; 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; 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:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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; 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|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:UP000248483};
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 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 280..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 325..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 909..930
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 963..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1001..1022
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1034..1060
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1072..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 21..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 848..1099
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1167 AA; 134387 MW; 92357E30FC8F2433 CRC64;
MSVFEKESED KQNGEQERYL QANNREFNSL FGYPNNSIKT SKYNAFNFLP MNLFEQFQRL
ANAYFLFLLF LQLIPQISSL AWYTTVVPLM VVLSITAVKD AIDDVKRHQN DNQVNSRSVL
LLMDGRIVTD KWMNVQVGDI IKLENNQVVT ADILLLSSSE PYSLTYIETA ELDGETNLKV
KQAISVTSEM EDNLKLLSAF DGEVRCESPN NRLDRFTGIL IYKGKNYVLD HDRLILRGCI
IRNTDWCYGL VIFTGPDTKL MQNSGKSTFK RTHIDHLMNV LVLWIFLFLG SMCFVLAVGH
CIWESKKGYY FQDFLPWKEY VSSSAVSAVL IFWSYFIILN TVVPISLYVS VEIIRLGNSF
YINWDRRMFY ELKNTPARAC TTTLNEELGQ VKYVFSDKTG TLTQNIMIFN KCSINGKFYG
VVYDKNGQRV EVSEKTEKVD FSYNRLADPK FSFYDKTLVE AVKRGDRWVH LFFLSLSLCH
TVIPEEKVEG ELTYQAQSPD EGALVTAARN FGFVFRSRTS ETIMVVEMGE TRIYQLLAIL
DFNSVRKRMS VIVRTPEDRV MLFCKGADTI LCQLLHPSCR SLRDVTMEHL DDFASDGLRT
LMVAYRELDN AFFQDWSRKH SEAYLSLENR EDKISMVCEE IEKDLMLLGA TAIDDKLQDG
VPETIITLNK AKIKIWVLTG DKQETAVNIA YACNIFEDEM DGMFIVEGKD DETVRQELRS
AREKMKPESL LESDPVNSYL TTNPRMPFKI PEEMPNGNYG LIINGYSLAH ALEGNLELEL
LRTACMCKGV ICCRMTPLQK AQVVELVKRY KKAVTLAIGD GANDVSMIKA AHIGVGINGQ
EGMQAMLNSD YAFSQFRYLQ RLLLVHGRWS YNRMCKFLSY FFYKNFAFTL VHFWYAFYSG
FSAQTVYDTW FITFYNLVYT SLPVLGLSLF DQDVNETWSL RFPELYEPGQ HNLYFNKKEF
VKCLMHGIYS SLVLFFIPMG TVYNSVRSDG KEISDYQSFS MIVQTSLLCV VTVQIALETT
YWTMISHIFT WGSLGFYFCI LFFLYSDGLC LMFPNIFQFL GVARNTLNLP QMWLSIVLSV
VLCMLPVIGY QFLKPLFWPV SVDKIIDRIH HCMRHPLPHP SRTKWKHASS QRSAYAFSHK
QGFGALITSG KTMRAKMSKK NSFPFKK
//