ID A0A3B4ZY66_9TELE Unreviewed; 1205 AA.
AC A0A3B4ZY66;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSSPAP00000013275.1};
GN Synonyms=atp11a {ECO:0000313|RefSeq:XP_008279269.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000013275.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000013275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008279269.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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_008279269.1; XM_008281047.1.
DR AlphaFoldDB; A0A3B4ZY66; -.
DR STRING; 144197.ENSSPAP00000013275; -.
DR Ensembl; ENSSPAT00000013498.1; ENSSPAP00000013275.1; ENSSPAG00000009986.1.
DR GeneID; 103356762; -.
DR CTD; 23250; -.
DR GeneTree; ENSGT00940000157849; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; 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; 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:UP000694891};
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 1132..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 138002 MW; B93FE70FC6456D18 CRC64;
MGMDFSTLRT LISRYCVGEE NWVDSRTIYI GHKEPPPGTE AFIQQRFPDN RIVSSKYTFW
NFIPKNMFEQ FRRVANFYFL IIFLVQLIID TPTSPITSGL PLFFVITVTA IKQGYEDWLR
HKADNAVNKC PVHVVQHGKV VRKQSRKLRV GDVVLVKEDE SFPCDLILLS SSRDDGTCFV
TTASLDGESS HKTYYAVQDT KAYNTEKEVD SIHATIECEQ PQPDLYKFVG RINVYMDNEP
VARPLGSENL LLRGATLKNT EYIYAVAIYT GMETKMALNY QSKSQKRSAV EKSMNAYLVV
YLCILISKAV INTVLKYAWQ ADPNRDEPWY NERTEVERQR HVLIRAFTDF LAFMVLFNYI
IPVSMYVTVE MQKFLGSYFI MWDDEMFDEE LGERAVVNTS DLNEELGQVE YVFTDKTGTL
TENNMEFIEC CVDGHVYVPH VICNGQVMPG AAGMDMIDTS PGPKAREHEE LFFRALCLCH
TVQVKEEETV DGIKHGIHQG KSSSFYISSS PDEVALVEGM KRLGFTYLRL KDGQMEILNR
EDEIERFELL EVLTFDSVRR RMSVIVRSNS GELYLFCKGA DSSIFPRVIS GKVDQVRARV
EHNAVEGLRT LCVAYRPLSP EQYQEVCHLL SSAKLALQDR DKRLAEAYDL IEKDLILLGA
TAVEDRLQEK AADTIESLHK AGMKVWVLTG DKMETAAATC YASKLFRRNT QILELTTKRT
EEQSLHDVLF DLSRTVLRQH GGMTRDTFSG LSGDCTDYGL IIDGATLSAV MRPGQEDSNS
GNYKEIFLEI CRNCSAVLCC RMAPLQKAQI VKLIKASKEH PITLAIGDGA NDVSMILEAH
VGIGIMGKEG RQAVRNSDYA IPKFKHLKKM LLVHGHYYYI RISELVQYFF YKNVCFIFPQ
FLYQFFCGFS QQPLYDTAYL TLYNISFTSL PILLYSLIEQ HINMDILKKD PSLYRDIAKN
SLLRWPIFIY WTILGVYDAI VMFFGAYFLF DNTTFTSNGQ MFGNWTFGTL VFTVLVFTVT
FKLALDTHYW TWINHFVIWG SLIFFVVFSL LWGGIIWPFL NYQRMYYVFM QMLSSGPAWL
SIILLITASL LPDVVKKVIW RALWPTTTER IQNADKLYKG QLSEFTPLAS LHAPPKASSH
RRGSENQRNI PNPRRSETFT KKIMFTRWQR APDYCTFTPL LRFADGSRQP KQGHAYSGAG
PETSV
//
