ID A0A667WYK5_9TELE Unreviewed; 1104 AA.
AC A0A667WYK5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005006723.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005006723.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A667WYK5; -.
DR Ensembl; ENSMMDT00005006898.1; ENSMMDP00005006723.1; ENSMMDG00005003653.1.
DR GeneTree; ENSGT00940000157110; -.
DR Proteomes; UP000472263; 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:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING 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:UP000472263};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1104
FT /note="Phospholipid-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025372355"
FT TRANSMEM 280..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 323..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 842..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 889..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..104
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 776..1018
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1104 AA; 124272 MW; 4561FFD6AF683C18 CRC64;
MPTTMLCFLE SLLFSHSVGY EKTEDASEKT SLADQEDARL IFLNQPQFTK FCSNRVSTAK
YNFLTFLPRF LYSQFRRAAN SFFLFIALLQ QIPDVSPTGR WTTLVPLLFI LVVAAVKEVI
EDLVRKTTIV HWEKVAVGEV VRAANGDHLP ADLVILSSSE PQGMCYIETS NLDGETNLKI
RQGLQSTAEI KDIDSLMRLS GRMECESPNR HLYEFVGNIR LDGHSTVPLG PDQILLRGAQ
LRNTQWVHGI VVYTGHDTKL MQNSTRPPLK LSNVERITNF QILVLFGCLL AISLVCSIGQ
TIWKYQYGNA AWYMDLNYGG AANFGLNFLT FIILFNNLIP ISLLVTLEVI KFVQAFFINW
DTDMHYEPTN TPAMARTSNL NEELGQVKYI FSDKTGTLTC NVMQFKKCTI AGVAYGHSTQ
SSEEAGFNDP SLLENLQSNH PTAAVILEFM TMMAICHTAV PEHTDGKITY QAASPDEGAL
VRAARNLGFV FSGRTPDSVI VEMRMSVIMR TPSGKIRLYC KGADTVIYDR LADSSRYKEI
TLKHLEQFAT EGLRTLCFAV ADISESSYQQ WQEVHHRACT SMQNRALKME ESYELIEKNL
QLLGATAIED KLQDKVPETI ETLIKADIKI WILTGDKQET AINIGHSCKL LTKNMGMLVI
NEDTLDGTRE TLSHHCGMLG DALYKENDFA LIIDGKTLKY ALTFGARQYF LDLALSCKAV
ICCRVSPLQK SEVVEMVKKQ VKVITLAIGD GANDVGMIQT AHVGVGISGN EGLQAANSSD
YSIAQFKYLK NLLLVHGAWN YNRVAKCILY CFYKNIVLYI IEIWFAFVNG FSGQILFERW
CIGLYNVIFT ALPPLTLGIF ERSCRKENML KYPELYKTSQ NAMGFNTKVF WAHCLNGLFH
SVILFWFPLK AFQHDTVFGN GKTPDYLLLG NMVYTVSSPV FLRHSFSHIA IWGSIGLWVV
FFVIYSSLWP LIPLAPDMSG EAEMMFNSGV FWMGLFFIPV TSLVFDVAYK VVKKVCFKTL
VDEVQELEAL SKDPGAVVHG KSLTERAQLL KNVFKKSTVS LYRSDSMQQN LLHGYAFSQD
ENGVVSQSEV IRAYDTTKQR TNEW
//
