ID A0A3Q3EIP8_9LABR Unreviewed; 1184 AA.
AC A0A3Q3EIP8;
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};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000007278.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000007278.1}
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; A0A3Q3EIP8; -.
DR STRING; 56723.ENSLBEP00000007278; -.
DR Ensembl; ENSLBET00000007657.1; ENSLBEP00000007278.1; ENSLBEG00000005570.1.
DR GeneTree; ENSGT00940000165692; -.
DR InParanoid; A0A3Q3EIP8; -.
DR Proteomes; UP000261660; 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; 1.
DR PANTHER; PTHR24092:SF46; PHOSPHOLIPID-TRANSPORTING ATPASE ID; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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:UP000261660};
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 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 331..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 865..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 948..971
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1017..1038
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1058..1081
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 22..88
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 834..1087
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1162..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 133494 MW; 11CDF40CDE0A89CD CRC64;
MVSELHRAAL CRKDALEEER RVRANDREYN DKFQYASNCI MTSKYNIITF LPVNLFEQFQ
EVANTYFLFL LILQLIPQIS SLSWFTTIVP LALVLSITAV KDATDDYFRH NSDNQVNNRQ
SQVLIRGSLQ NEKWMNVRVG DIIKLENNQF VAADLLLLSS SEPHGLCYIE TAELDGSENT
PHLSIKSELR QSVSVTSELG DQNNLASFNG EVVCEPPNNK LDRFCGTLYW RDKKYTLTNQ
NMLLRGCVLR NTEACYGLVI FAGPDTKLMQ NSGRTKFKRT SIDRLMNTLV LWIFGFLVCM
GVILAVGNAV WEREVGSLFQ SYLPWDPPVD NFLFSAFLSF WSYVIILNTV VPISLYVSVE
VIRLGHSYFI NWDQQMFCSQ CNTAAEARTT TLNEELGQVE YIFSDKTGTL TQNIMSFNKC
SINRQTYGNI HFTHLFVLGE RLDFTPFNPL ADPDFCFYDD TLLESVKVGD SHTHEFFRLL
SLCHTVMSEE KSEGELIYKA QSPDEGALVT AARNFGFVFR SRTPGTITTT EMGRPVTYTL
LAILDFNNIR KRMSVIVRNP EGRIRLYCKG ADTVLLERLN PCNQELMNIT SDHLNEYASD
GLRTLALAYR DLSEDDWEMW SESHRCADKA TNCREDRLAA TYEAIEQDMM LLGATAIEDK
LQEGVPETIA VLSLANIKIW VLTGDKQETA VNIGYSCKML TDDMTEVFII SGHTVQSVRQ
ELRSVHLPLQ LSGVSNYGAV AHISGEFAIV INGHSLAHAL EADMETEFVL TACACKAVIC
CRVTPLQKAQ VVELIKKHKK AVTLAIGDGA NDVSMIKSAH IGVGISGQEG IQAVLASDYS
FSQFRFLQRL LLVHGRWSYL RMCRFLCYFF YKNFAFTMVH FWFGFFCGFS AQTVYDQYFI
TLYNIVYTSL PVLAMGIFDQ DVPDQRSLEY PKLYEPGQLN LLFNKREFFI CIAQGIYTSV
VLFFVPCAVL SDATQSTGVP LADYQTFAVT TATALVIVVS VQIALDTGFW TVINHVFVWG
SLGCYFAIMI ALHSQTLFRI FPNQFHFVGS AQSTLLQPVV WLTIALATAI CIVPVLAFRF
LKVDLKPQLS DTVRKVTQTQ CLLDGRLGAR GGSRRSGYAF AHQEGFGELI TSGKNMRLSS
LALANFASRH SSNWIDTLRR KKHNHTHTPP NASGDLGAPQ PYKL
//
