ID A0A3P9P4W2_POERE Unreviewed; 1202 AA.
AC A0A3P9P4W2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSPREP00000016839.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000016839.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000016839.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000016839.1};
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 RefSeq; XP_008424980.1; XM_008426758.1.
DR AlphaFoldDB; A0A3P9P4W2; -.
DR STRING; 8081.ENSPREP00000016839; -.
DR Ensembl; ENSPRET00000017019.1; ENSPREP00000016839.1; ENSPREG00000011298.1.
DR GeneID; 103475257; -.
DR CTD; 23250; -.
DR GeneTree; ENSGT00940000157849; -.
DR OMA; KAPDYCT; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011298; Expressed in caudal fin and 1 other cell type or tissue.
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; 3.
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 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:UP000242638};
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 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 296..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 918..938
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 968..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1002..1024
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1036..1060
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1066..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..98
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 854..1106
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1128..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 137849 MW; 5A228160E456C265 CRC64;
MGMDFSTLRT LISRYCAGEE NCVDTRTVYI GHKEPPPGAE AFIQQRFPDN RIVSSKYTFW
NFIPKNMFEQ FRRVANFYFL IIFLVQLIID TPTSPVTSGL PLFFVIIVTA IKQGYEDWLR
HKADKAVNQC LVQVVQHGKV SRKHSRKLTV GDVVYVKEDE SFPCDLILLS SSRDDGTCYV
TTASLDGESS HKTYHAIQDT KAYKTEEEVN YIHATIDCEQ PQPDLYKFRG NINIYMGNEP
VSRSLASQNL LLRGATLKNT EYIYGVAIYT GMETKMALNY QSKSQKRSAV EKSMNAFLVV
YLCILISKAV INTALKYVWQ ADPNRDEPWY NGKTESERQR HVLIRAFTDF LAFMVLFNYI
IPVSMYVTVE MQKFLGSYFI MWDDEMFDEE LGERAVVNTS DLNEELGQVE YVFTDKTGTL
TENNMEFIEC CVDGNVYVPH IICNGQVMPG AAGIDMIDTS PGPEAREREE LFFRALCLCH
TVQVKEEETV DGIKHGIHQG KSSSFYISSS PDEVALVEGM KRLGFTYLRL KDGQMEILNR
EDEIERFELL EVLTFDSVRR RMSVIVRSST GELYLFCKGA DSSIFPRVVS GKMEQIKARV
ERNAVEGLRT LCVAYRRLSP EQYEQVCHLL TRAKLEFQDQ DKLVAEAYDL IERDLILLGA
TAVEDRLQEK AADTIESLHK AGMKVWVLTG DKMETAAATC YASKLFRRST QILELTTKRT
EEQSLHDVLF ELSRTVLRHY GSMPRDASSG LSSEYIDYGL IIDGATLSAV MRPSQEDSNS
GNYKEIFLEI CRNCSAVLCC RMAPLQKAQI VKMIKSSKEH PITLAIGDGA NDVSMILEAH
VGIGIMGKEG RQAVRNSDYA IPKFKHLKKM LLVHGHYYYI RISELVQYFF YKNVCFIFPQ
FLYQFFCGFS QQPLYDTAYL TLYNISFTSL PILLYSLMEQ HINMDILKKE PTLYRDIAKN
SLLTWPIFIY WTVLGVYDAI VMFFGAYFLF DNTTFTSNGQ MFGNWTFGTL VFTVLVFTVT
FKLALDTHYW TWINHFVIWG SLVFFVVFSL LWGGIIWPFL NYQRMYYVFM QMLSSGPAWL
SIILLITASL LPDVVKKVFW RALWPTTTER IQSADKLYKG QLSEFTPLEA LHPPPRAGDH
QRSSGTQRNP RRSDTPNKKV MFTRWQRAPD YRTFTPLLRF TDGSRHSRPG NAYRGAGPET
SV
//
