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Database: UniProt
Entry: A0A2Y9QEC0_DELLE
LinkDB: A0A2Y9QEC0_DELLE
Original site: A0A2Y9QEC0_DELLE 
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}.
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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
//
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