ID A0A3Q2V321_HAPBU Unreviewed; 1368 AA.
AC A0A3Q2V321;
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000001513.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000001513.1}
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}.
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 STRING; 8153.ENSHBUP00000001513; -.
DR Ensembl; ENSHBUT00000013669.1; ENSHBUP00000001513.1; ENSHBUG00000002674.1.
DR GeneTree; ENSGT00940000156728; -.
DR OMA; FKVAREC; -.
DR Proteomes; UP000264840; 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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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:UP000264840};
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 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 121..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1121..1139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1199..1223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1230..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1257..1283
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1303..1321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 62..120
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1087..1323
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 643..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 153679 MW; 4E6716DD40BFBD26 CRC64;
MERLRWVQQC CRQLLAGDSR RGWYSDGLPT SSLLNTHSPR GRVCGKQRTV FPRNGRHQQD
YERVSRNYKS NAISTTKYTF LTFIPMNLFE QFHRAANLYF LFLTLLNWVP VVEAFQKEIT
MIPLLLVLII IAIKDALEDF RRYLFDKKVN NNVVRVFCGT QKSYVDQCWK NVQVGDFVHL
SCNEIIPADM LLLYSSDPHG VCYIETANLD GETNLKQRQV VSDFPLQGEE FTPESFHSRI
ECENPNNDLS RFRGYMEHSN GVRVGLHSGN LLLRSCTIRN TETVVGIVVY AGHETKAMMN
NSGPRYKRSK LEKHLNTDIL WCVVLLFVMC LTAAIGHGLW MNSFKESIFQ VDTETPPALA
GFYIFWTMVI VLQVLIPISL YVSIEIVKLG QIYFIHNDLS LYNKQLDSRI QCRALNITED
LGQIQYLFSD KTGTLTENKM VFRRCSIFGV EYPHEENARR LEVYESENTE TAVCSVTLKS
GYSGKSLSCR SLSCNRSSVS LHTLTAEPME EDQLSGHVQP RTGAFCSRMA KEVVPDPALG
RKLNWLTNHS SSETPSSMEL TYITDFFLAL AICNSVVVSS PNQPRHVIPE ERTPLKSLEE
VKLMFQRFSF SPFSALSPSQ IKGSPHSLKS RLFIRGKRGS LTLSTPVSNT TDVSSSSQEN
DSKPDLSARE EEEQDVEDQE TEDDLKDTQT NPDEARQSMQ DLTKQVEEIT DELVYEAESP
DEAALVHAAR AYRCTLRGRS AESLLVDLPG IGSLAIQLLH ILPFDSNRKR MSVVVRHPLT
GQVVVFTKGA DSVIMDLAES PTDQTEVYSH IKEKTQKHLD AYAREGLRTL CIAKKVLKED
EYDLWLKAHM LAESSIENRE ELLLESAQRL ETNLTLLGSH CSSDLNHSIS ELKYQHLKRM
RVFSGTTGIV DRLQEEVPET IAALQRAGIK VWVLTGDKQE TAINIAYACK LLCASDKLLT
ANCGSKDACA ALFEDLILEV QGGESLTALT GNGESMSSSF ILVIDGRTLG WALEDELRSN
FLELSRRCKA VICCRSTPLQ KSQVVQLIRD HLGVMTLAVG DGANDVSMIQ VADVGIGISG
QEGMQAVMSS DFAISRFKHL SKLLLVHGHW CYSRLANMIQ YFIYKNVMYV NLLFWYQFFC
GFSGSVMTNS WVLILFNLIF TSAPPLIYGI LNQDLPADAL MELPELYQDA QTSKTFVPYM
FWITVLDAFY QSLVCFFVPY FAYAGSDVGV LSFGSPINAS ALFIILLHQV IESNTLTWIH
MVVLVLSCTS YFGFVLLLSG FCVTCSPPVN PLGIELLQMS HSLFYITCVL TTVAALLPRY
AHTHTHCRNS CTGSVFPLGA LYNSLIIKSF TLTTPGDANV VITDTAIH
//
