ID A0A674E6E7_SALTR Unreviewed; 1150 AA.
AC A0A674E6E7;
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:ENSSTUP00000103635.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000103635.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000103635.1}
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; A0A674E6E7; -.
DR Ensembl; ENSSTUT00000111132.1; ENSSTUP00000103635.1; ENSSTUG00000045283.1.
DR GeneTree; ENSGT00940000157849; -.
DR Proteomes; UP000472277; 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:UP000472277};
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 72..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 967..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1031
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1043..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1073..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..96
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 853..1113
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1150 AA; 131702 MW; 04B18E1681BFE69C CRC64;
MDFSSIRKFI TRWCAGEENW VDTRTVYIGN KEPPPGAEAY IPQRYPDNRI ISSKYTFWNF
VPKNLFEQFR RIANFYFLII FLVQLIIDTP TSPITSGLPL FFVITVTAIK QGYEDWLRHK
ADNAINQCPV HEVQHGKVIR KQSRKLRVGD VVLIKEDETF PCDLILLSTS REDGTCFVTT
ASLDGESSHK TYYAVQDTKA FNTEEDFDTL QASIECEQPQ PDLYKFVGRI NIYSDRNEPI
ARPLGSENLL LRGATLKNTQ HIYAVAIYTG METKMALNYQ SKSQKRSAVE KSMNAYLIVY
LCILISKALI NTVLKYVWQA DPDKDEPFYN QKTDTERQRH ILIRAFTDFL AFMVLFNYII
PVSMYVTVEM QKFLGSYFIM WDDEMFDEEL GERAQVNTSD LNEELGQVEY VFTDKTGTLT
ENNMEFIECC VDGYVYVPDA ICNGQVMPGA TSMDMIDSSP GPGGKESEEL FFRALCLCHT
VQVKEEETVD GIKMGIHQNK ATSFYISSSP DEVALVEGMK RLGFTYLRLK DSHMEILNRE
DEVERFELLE VLTFDSVRRR MSVIVRSTTG EYYLFCKGAD SSIFPRVISG KVEQVKARVE
HNAVEGLRTL CVAYRKLSVT QYEETCHLLN SAKLALQDRD RKLAEAYDLI EKDFILLGAT
AVEDRLQDKA ADTIESLQKA GMKVWVLTGD KMETAAATCY ASKLFRRSTQ ILELTTKRTE
EQSLHDVLFD LSKTVLRQHG SMTRDTFSGL SADCVDYGLI IDGATLSAVL KPSQEDSSQG
NYKEIFLEIC RNCSAVLCCR MAPLQKAQIV KLIKSSPEHP ITLAIGDGAN DVSMILEAHV
GIGIMGKEGR QAARNSDYAI PKFKHLKKML LVHGHYYYIR ISELVQYFFY KNVAFIFPQF
LYQFFCGFSQ QPLYDTAYLT LYNISFTSLP ILLFSLIEQH INMDILKKDP SLYRDIAKNS
LLRWPIFIYW TFLGVFDAVV FFFGSYFLFN NSTFTSNGQL MTTNTQMMFG NWTFGTLVFT
VLVFTVTLKL ALDTHYWTWI NHFVIWGSLL FFVIFSLLWG GIIWPFLNYQ RMYYVFIQML
SSGPAWLSII LLIVISLLPD VVKKVVCRAL WPTTTERIQR MRADRNFDGV MTYSRDSLLD
GGVALSTSEA
//
