ID A0A663FK08_AQUCH Unreviewed; 1087 AA.
AC A0A663FK08;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP11A {ECO:0000313|Ensembl:ENSACCP00020024007.1};
OS Aquila chrysaetos chrysaetos.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Aquila.
OX NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020024007.1, ECO:0000313|Proteomes:UP000472275};
RN [1] {ECO:0000313|Ensembl:ENSACCP00020024007.1}
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; A0A663FK08; -.
DR Ensembl; ENSACCT00020025072.1; ENSACCP00020024007.1; ENSACCG00020016228.1.
DR GeneTree; ENSGT00940000157849; -.
DR Proteomes; UP000472275; 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; 2.
DR PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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:UP000472275};
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 62..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 277..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 847..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 927..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..983
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 995..1019
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1025..1050
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 32..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 813..1065
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 585..612
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1087 AA; 125662 MW; E10BA9DB01C4F045 CRC64;
VFQRTQKENW VDSRTIYVGH REPPPGTEAY IPQRFPDNRI VSSKYTFWNF VPKNLFEQFR
RIANFYFLII FLVQLIIDTP TSPVTSGLPL LFVITVTAIK QGYEDWLRHK ADNAMNQCPV
HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSS RGDGTCFVTT ASLDGESSHK
TYYAVQDTKA FHNEQEIDAL HATIECEQPQ PDLYKFVGRI NVYHDRNEPT LLYRAIVSKI
SCLISGVAIY TGMETKMALN YQAKSQKRSA VEKSMNVFLI VYLCILISKA LINTVLKYVW
QSEPFRDEPW YNQKTEPERK RNLFLRAFTD FLAFMVLFNY IIPVSMYVTV EMQKFLGSYF
LTWDEEMFDE DTGEGPLVNT SDLNEELGQI EYVFTDKTGT LTENNMEFVE CCIEGHVYVP
HCINTISYFD HTLHYEELFF RALCLCHTVQ VKDDDSVDGL KKNQLSRRSC IYISSSPDEV
ALVEGIQRYV CNQDNFMEIL NRENNIEKFE LLEVLSFDSV RRRMSVIVKS STGDIFLFCK
GADSSIFPRV KEGKIDQVRS RVERNAVEGL RTLCVAYKKL TAEEYSNAQK LLQNAKLALQ
DREKKLAEVY EKIERDFILL GATAVEDRLQ EKAADTIEAL QKAGIKVWVL TGDKMETAAA
TCYACKLFRR NTQILELTTK KIEEQSLHDV LFDLSKTVLR HNVYILSLNR LSTDMQDYGL
IIDGAALSLI MKPRQDGSSA NYRELFLEIC RNCSAVLCCR MAPLQKAQIV KLIKLSKEHP
ITLAIGDGAN DVSMILEAHV GIGIIGKEGR QAARNSDYAI PKFKHLKKML LVHGHFYYVR
ISELVQYFFY KNVCFIFPQF LYQFFCGFSQ QTLYDTAYLT LYNISFTSLP ILLYGLMEQH
VSADTLKREP SLYRDVAKNA LLRWRAFIYW TFLGVFDAVV FFFGAYFLFD NTVVTSNGQM
FGNWTFGTLV FTVLVFTVTL KLALDTHYWT WINHFMIWGS LVFYIIFSLL WGGIIWPFLN
YQRMYYVFMQ MLSSGPAWLG IILLITVSLL PDVLKKVLCR QLWPTATERI QVKIFFIVKL
VFCITSL
//
