ID A0A4Z2HK19_9TELE Unreviewed; 840 AA.
AC A0A4Z2HK19;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP9A_0 {ECO:0000313|EMBL:TNN65264.1};
GN ORFNames=EYF80_024553 {ECO:0000313|EMBL:TNN65264.1};
OS Liparis tanakae (Tanaka's snailfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Liparidae; Liparis.
OX NCBI_TaxID=230148 {ECO:0000313|EMBL:TNN65264.1, ECO:0000313|Proteomes:UP000314294};
RN [1] {ECO:0000313|EMBL:TNN65264.1, ECO:0000313|Proteomes:UP000314294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:TNN65264.1};
RA Kim W., Song I., Jeong J.-H., Kim D., Kim S., Ryu S., Song J.Y., Lee S.K.;
RT "First draft genome of Liparis tanakae, snailfish: a comprehensive survey
RT of snailfish specific genes.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TNN65264.1}.
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DR EMBL; SRLO01000238; TNN65264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z2HK19; -.
DR Proteomes; UP000314294; Unassembled WGS sequence.
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 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; 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:SF49; PHOSPHOLIPID-TRANSPORTING ATPASE IIA-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 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:UP000314294};
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 126..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 704..726
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 782..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 644..834
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 840 AA; 94170 MW; 7ED45B08AC6747CC CRC64;
MIFLRTSERN GSCFLRTDQL DGETDWKLRL PVACTQRLPT AADLLQIRSY VYAEEPNIDI
HNFTGTFTRE DGDPPVNESL SIENTLWAST VVASGTVVGV VIYTGKELRS VMNTSNPRHK
VGLFDLEVNC LTKILFGALM MVSLVMVALQ HFTGRWYLQI VRFLLLLSNI VPISLRVNLD
MGKMVFSWMI KKDSKIPGTM VRSSTIPEQL GRISYLLTDK TGTLTQNEMV FRRLHLGTVA
YGMDSMDEVQ SLVFSAYTQP AHDLSASRAP AATKVRKTII SRVHEAVKAI ALVHNVTPVY
EANGVTDQAE AEQHYEDTCR VYQASSPDEV SLVQWTESVG LTLVGRDHSS MQLRTPTGQI
LNFTILQIFP FTYESKRMGV IVRDESTGEI TFYMKGADVV MAGIVQYNDW LEEECGNMAR
EGLRVLVVSK KSLTEEQYQD FEASRRPARY VQAKLSVHDR SLKVATVIES LEMEMELLCL
TGVEDQLQTD VRPTLEILRN AGIKVWMLTG DKLETATCTA KNAHLITRNQ DIHIFRPVTT
RGEAHLELNA FRRKHDCALV ISGDSLEVCL KYYEYEFMEL ACQCPAVVCC RCTPTQKAQI
VRLLQERTGK LTCAVGDGGN DVSMIQEADC GVGVEGKEGK QASLAADFSV TQFKHLGRLL
MVHGRNSYKR SAALSQFVIH RSLCISTMQA VFSSVFYFAS VPLYQGFLII GYSTIYTMFP
VFSLVLDKDV KSEVAMLYPE LYKDLLKGRP LSFKTFLIWV LISIYQGGII MYGALLLFDS
EFVHAVAISF TALILTELLM VALTIQTWHW LMIVGELLSL ACYVASLVFL HEFIACQAIG
//
