ID A0A6Q2ZD16_ESOLU Unreviewed; 1086 AA.
AC A0A6Q2ZD16;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B4 {ECO:0000313|Ensembl:ENSELUP00000075758.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000075758.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000075758.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000075758.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A6Q2ZD16; -.
DR Ensembl; ENSELUT00000067478.1; ENSELUP00000075758.1; ENSELUG00000005425.2.
DR GeneTree; ENSGT00940000160101; -.
DR Proteomes; UP000265140; LG19.
DR Bgee; ENSELUG00000005425; Expressed in pharyngeal gill and 11 other cell types or tissues.
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:SF80; PHOSPHOLIPID-TRANSPORTING ATPASE IM-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000265140};
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 254..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 792..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 875..894
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 914..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 947..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 988..1011
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 11..76
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 761..1018
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1086 AA; 123066 MW; EEA822D30EC55D95 CRC64;
MDNAVEEERH VRANDRNYND KFFYADNHIK TSKYNVFTFL PINLFEQFQR VANAYFLVLL
ILQLIPEISS LPWVTTTVPL VMVLVITAVK DATDDYVSHL QNEKWMNVRV GDIIKLENNQ
FVAADILLLS SSEPYGLCYI ETAELDGETN LKVRQALTVT SELGADILKL AEFNGEVICE
APNNKLDKFK GTLYWRGSKF PLDNEKMLLR GCVLRNTDWC FGMVIFAGLQ TKLMQNCGRT
TLKRTSIDKL MNTLVLWIFG FLVCMGVILA IGNTIWEQEV GRSFQVYLPW ERPVSNNNAV
FSGFLTFWSY IIILNTVVPI SLYVSVEVIR LGHSYFINWD GKMYYGQKDT PAEARTTTLN
EELGQVEFIF SDKTGTLTQN IMVFNKCSIN GNTYGDVYDE FGHKRTACVD FSFNPLSDRK
FTFHDSSLVE AIKMEEPSVQ EFFRLLALCH TVMSEEKNEG DLLYQAQSPD EGALVSAARN
FGFVFRSRTP ETITLYEMGT AVTYQLLAIL DFNNVRKRMS VIVRNPAGQT KLYCKGADTI
IFDRLDPSNE DLMDTTSEHL NEFAGEGLRT LALAYKVLDR DFFEEWMTRL LLASTVMENR
EQRLADLYEE IETGLLLLGA TAVEDKLQEG VPETIACLTL ANIKIWVLTG DKLETAMNIG
YSCNMLRDDM NEVFIISGHT AAEAHALEPE LEQVLLETAC LCKTVICCRV TPMQKAQVVE
LVKTNKMAVT LAIGDGANDV SMIRTAHIGV GISGQEGMQA VLASDYSFAQ FRYLQRLLLV
HGRWSYFRMC NFLFYFFYKN FAFTLVHFWF GFFCGFSAQT VYDQWFITLF NIVYTSLPVL
AMGLFDQDVN EANSHRYPGL YRPGQLNLLF NKRQFFLCTL QGIVTSFLLF FVPYGAFSLG
VRADGLHLSD QQSFAVTIAT SLVIVVIAFQ SDIGLDTYYW TAVNHLFVWG SLAVYFAILL
AMQSDGLFSI FPSQFPYIGT ARSCLAQWSV WLVILLTTAV CVLPGMAVRF LKTDLYPTLT
DKVQGPREQN LRRVRRTSSR RSGYAFSHQQ GYGELITSGK NMKVAPALLV HPLAYPPLGF
VTADIF
//
