ID A0A3Q1KD09_ANATE Unreviewed; 1162 AA.
AC A0A3Q1KD09;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-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=ATP11B {ECO:0000313|Ensembl:ENSATEP00000032576.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000032576.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000032576.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1KD09; -.
DR STRING; 64144.ENSATEP00000032576; -.
DR Ensembl; ENSATET00000033052.2; ENSATEP00000032576.1; ENSATEG00000022414.2.
DR GeneTree; ENSGT00940000156162; -.
DR InParanoid; A0A3Q1KD09; -.
DR OMA; HGHTAYQ; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000265040; 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; 3.
DR PANTHER; PTHR24092:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 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:UP000265040};
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 66..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 342..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 839..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 937..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 971..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1006..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1036..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 36..90
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 823..1076
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1162 AA; 132203 MW; FFEB93E04F6ECFE8 CRC64;
MLRWIRQQLG FDPPHQSETR TVYVANRFPQ HCHYIPQRFA DNRIISSKYT IWNFVPKNLF
EQFRRIANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHKADNEVN
GAPVFVVRSG SLVQTRSKNI RVGDIVRVAK DETFPADLVL LSSDRADGTC HITTASLDGE
TNLKTHYSVA ETSVCQSVSQ LEALQAVVEC QQPEADLYRF VGRITVTQRG EEIVRPLGPE
NLLLRGARLK NTKEIYGVAV YTGMESKMAL NYKCKSQKRS AVEKSMNSFL IIYLGILLFE
AVLSTILKYA WQAENKWDEP FYNQKTEQQR NSSPILKFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
ECSINGTKYR EVNGKLVPEG MTDDSPDGSI PHLTGEELLF LKAVSLCHTV QISYDQPDCL
VAGGDPFSHA NGFSSNNMEY YASSPDEKAL VEATKRIGVA FACSSGDTME IKAFGKSEKY
KLLHVLEFDA DRRRMSVILQ TPSGGKVLFT KGAESAILPF TTSGEIEKTR LHVDEFALKG
LRTLVVACRH FSPEEYIDVD KRLNSARTAL QQREERLQEA FSYIEKDLQL LGATGVEDKL
QDKVQETIEA LRLAGIKVWV LTGDKHETAV SVSLSCGHFH RTMNILELLQ QRSDNECAEQ
LRRLAKRIKE DHVIQHGLVV DGASLSLALR EHEKLFMEVC KNCSAVLCCR MAPLQKAKVV
RLLKTSPEKP ITLAIGDGAN DVSMIQEAHV GIGIMGKEGR QAVRNSDYAI ARFKFLAKLL
LVHGHFYYIR IATLVQYFFY KNVCFITPQF LYQFFCLFSQ QTLYDSVYLT LYNICFTSLP
ILVYSLFEQL VHPHVLQNKP GLYRDISKNS LLSFRTFLYW TMLGFCHAFV FFFGSYILMG
EDTTLMGNGQ MFGNWTFGTL VFTVMVITVT LKLALETHFW TWMNHFVTWG SIAFYFIFSL
FYGGIIWPFL HTQDMYFVFV QLLSSGSAWF AIIIIVITCL FPDVVKKVFY RHLQPTSTQK
SQSLSAPQAQ ALSCMESLCC YQHGQSGCSR LARFLEQMTG QCQATNHCHA SSRSNRSWSD
TETFYSNDRS ILTLSPIEAT HC
//
