ID A0A1V4KQQ7_PATFA Unreviewed; 1279 AA.
AC A0A1V4KQQ7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B3 {ECO:0000313|EMBL:OPJ86762.1};
GN ORFNames=AV530_006866 {ECO:0000313|EMBL:OPJ86762.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ86762.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ86762.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ86762.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ86762.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ86762.1}.
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DR EMBL; LSYS01002182; OPJ86762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KQQ7; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:SF78; PHOSPHOLIPID-TRANSPORTING ATPASE IK; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000190648};
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 386..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 429..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1021..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1071..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1106..1127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1134..1153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1181..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 116..190
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 958..1200
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 721..748
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1279 AA; 142996 MW; 19F2859A9DCDB475 CRC64;
MSPETPNFLV DAAPGPGTSP AGAAGATVAL EELPGNSRSY RQPTAAPHRC SSPGDLGDQR
DRTFPARPAQ PVHSSAELEE RPAGAARGAG MAEQDPASSR PRGKRHRPAF TWEVRANDRN
YHTQFRKKSA FCLTKKKYAG NAISTAKYNV LTFLPLNLYE QFHRAANVYF VLVILLQAFP
EISTLPWYTL LFPLSCLLAI RGLRDLIDDI GRHQSDRSIN SRPCEILSGK SFRWQKWRDI
CVGDIVRLRK ESLVPADMLL LRSSEPSSLC YLETADIDGE TNLKFRQALL VTHRELASEE
SMAAFDGRVT CEEPNSRMHS FTGTLAWRGE THALDSERLL LRGCRLRNTD LCYGLVIYAG
FDSKIMRNCG KIKRKKTKLD RMMDRLVIMI FLALLVTSLC LAIASGFWAK TFQEKHGYLS
VFYKHTTPAQ QAFFSFWGFT ILLSIIIPMS MYITFEFIYL VNSFFINWDL EMYHAAKDIP
AKARSTSLND QLGQIEYIFS DKTGTLTQNV MSFKKCCING TIYGAGAGCG SKHPSGSGLT
RSHRGEQKSD FCDARLLEAA RRDSDPALRE FLRLLALCHT VMVEERGDQL VYQAASPDEE
ALVLAARSLG YIFLSRTQDT ITISELGMKR TYKVLAMLDF NSDRKRMSVL VRDPQGTIRL
YTKGADTVIL ERLQRRGPRE TFTEMALDRF AEETLRTLCL ASKEVSEAEY GAWSRRHHEA
SVLLQDRARE LDRLYDEMEQ NLQLLGATAI EDKLQDGVPE TIQLLKLGNI KVWVLTGDKQ
ETAMNIGYAC KLLTDDMEVL EEKKVSEILG ALRASSSGLA GSAGPLCHGR LSQQRPEASQ
CKKRALVISG DFLDKILRTG EALKEEGRLR RWLPCRGAAG SPEEAGLAEK AFVELAASCQ
AVLCCRVTPR QKALIVQLVK KHKKATTLAI GDGANDVNMI KTADIGVGIS GLEGLQAVQC
SDYALAQFSY LQRLLLVHGR WAYLRICKFL RCFFYKTFAG LMTQVWFAFH SGFTAQPLYE
GWFLALYNIF YTAYPILSLG LLEQDVSAKK SLEFPELYVI GQQDELFNYR VFSITVLHGL
STSLASFYIA LWAFEDRVGS RAVGDYESFA ITVATSALLS VLMEIILDTK FWTLLSFLMV
TTSLLLFCLF SFLTQSIDAF RIAPAIFRFP DASWNALTDP YVLLVVLLSL VVNTIPSLTK
IRLKAQREPE PLVELRAHVL RGSFHHRSSY AFSHQEGYAG LITRGDSLRS RGTRSTIQHP
DTAPALSPGP SSPMPSPSA
//
