ID A0A093CIY8_9AVES Unreviewed; 1029 AA.
AC A0A093CIY8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=N339_05523 {ECO:0000313|EMBL:KFV12307.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV12307.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV12307.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV12307.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL241599; KFV12307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CIY8; -.
DR Proteomes; UP000053149; 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; cd07541; P-type_ATPase_APLT_Neo1-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:SF49; PHOSPHOLIPID-TRANSPORTING ATPASE IIA-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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; 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:UP000053149};
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 84..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 280..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 932..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1012
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 28..87
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 794..1021
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV12307.1"
FT NON_TER 1029
FT /evidence="ECO:0000313|EMBL:KFV12307.1"
SQ SEQUENCE 1029 AA; 116869 MW; E478BE20F7F80243 CRC64;
CCFHRCCECL RCCGRRDPRP RTVWLGHPEK RDQRYPRNVI NNQKYNFFTF LPGVLFNQFK
YFFNLYFLLL ACSQFVVEMR LGALYTYWVP LGFVLAVTII REATEEIRCY MRDKEVNSQI
YSKLTARGTV KVKSSNIQVG DLIIVEKNQR VPADMIFLRT SEKNGSCFLR TDQLDGETDW
KLRLPVTCTQ RLPTASDLLQ IRSYVYAEEP NIDIHNFVGT FTREDSDPPM NESLSIENTL
WASTVIASGT VVGVVLYTGR ELRSVMNTSN PRSKIGLFDL EVNCLTKILF GALVVVSLVM
VALQHFAGRW YLQIIRFLLL FSNIIPISLR VNLDMGKIVY SWVIRRDSKI PGTVVRSSTI
PEQLGRISYL LTDKTGTLTQ NEMVFKRLHL GTVAYGLDSM DEVQSHIFSI YTQQSQDPPA
VKGLTLATKV RKTMSSRVHE AVKAIALCHN VTPVYESNGV TDQAEAERHY EDSCRVYQAS
SPDEVALVQW TESVGLTLVG RDQSSMQLRT PGGHILNFTI LQIFPFTYES KRMGIIVRDE
STGEITFYMK GADVVMAGIV QYNDWLEEEC GNMAREGLRV LVVAKKSLTE EQYQDFEARY
VQAKLSVHDR SLKVATVIES LEMEMELLCL TGVEDQLQTD VRPTLETLRN AGIKVWMLTG
DKLETATCTA KNAHLVTRTQ DIHIFRLVTN RGEAHLELNS FRRKHDCALV ISGDSLEVCL
KYYEYEFMEL ACQCPAVVCC RCAPTQKAQI VRLLQERTGK LTCAVGDGGN DVSMIQEADC
GVGVEGKEGK QASLAADFSI TQFKHLGRLL MVHGRNSYKR SAALSQFVIH RSLCISTMQA
VFSSVFYFAS VPLYQGFLII GYSTIYTMFP VFSLVLDKDV KSEVAMLYPE LYKDLLKGRP
LSYKTFLIWV LISIYQGSII MYGALLLFES EFVHIVAISF TSLILTELLM VALTIQTWHW
LMIVAELLSL SCYIASLVFL HEFIDVYFIA TLSFLWKVTV ITLVSCLPLY VLKYLRRRFS
PPSYSKLTS
//
