ID A0A3Q2VMV5_HAPBU Unreviewed; 1130 AA.
AC A0A3Q2VMV5;
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};
GN Name=ATP11C {ECO:0000313|Ensembl:ENSHBUP00000012945.1};
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:ENSHBUP00000012945.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000012945.1}
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 RefSeq; XP_005913296.1; XM_005913234.2.
DR AlphaFoldDB; A0A3Q2VMV5; -.
DR Ensembl; ENSHBUT00000032751.1; ENSHBUP00000012945.1; ENSHBUG00000014903.1.
DR GeneID; 102289938; -.
DR CTD; 286410; -.
DR GeneTree; ENSGT00940000158878; -.
DR OrthoDB; 275833at2759; -.
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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 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: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 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 973..995
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1010..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1041..1062
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1082..1104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 38..91
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 859..1106
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1130 AA; 129645 MW; 0683D2ACF9D94E4B CRC64;
MLRRRLNRWF GGEDRRVGSR TIYVGHRPCP ANEVFIPPKF CDNRIVSSKY TVWNFLPKNL
FEQFRRIANF YFLIIFLVQV IVDTPTSPVT SGLPLFFVIT VTAIKQGYED WLRHKADNEV
NKYRVTVLED GRRIQKESEK IKVGDVLEVE EDETFPCDLI LLQSSRDDGT CFVTTASLDG
ESNHKTHYTV PDTERDVESL NATIECEQPQ PDLYKFVGRM HIYKNNEEPS LRSLGPENLL
LKGATLKNTQ SICGVAVYTG METKMALNYQ GKSQKRSVVE KSINAFLLVY LCILVSKALV
CTTLKYVWQS KPGQDEPWYN EKTLKEKETN LYLNMFTDFL SFMVLFNFII PVSMYVTVEM
QKFLGSFFIS WDKDFFDSEI EEGALVNTSD LNEELGQVEY VFTDKTGTLT QNNMEFIECC
IDGHQYKYRD ASSEVDGFCV TDGPMNTVQQ KAGREREELF LRALCLCHTV QVKESTEQGQ
GQDGRIDQVD GLMVDGQVVP PLQEQRGFIA SSPDEIALVQ GAMRYGFTFL GLESKTMKIL
NRTNDVEMYE LLHVLNFDPV RRRMSVIVRS ISGETLLFCK GADSSIFPRV KQEEVEKIRM
HVERNATDGY RTLCVAYKHL TAEEYDQVDS GLREARLALQ DREEKLMAVY NQVETGMNLI
GATAVEDRLQ EEAAETMEAL QGAGIKVWVL TGDKMETAKS TCYACRLFKR NTELLELTVR
TLESPGKRRE DRLHDLLLEY HKKTVQDAPP AKTRVARNWS SQDYGFIVDG ATLSMVLNSS
SENNLHDYKD LFLQICQNCT SVLCCRMAPL QKAQIVKMVK NSKGSPITLS IGDGANDVSM
ILEAHVGIGI KGKEGRQAVR NSDYAIPKLK HLKKLLLGHG HLYYVRIAHL VQYFFYKNLC
FILPQFLYQF FCGCSQQPLY DAAYLTMYNI CFTSMPILAY SLFEQHISIE MLLENATLYR
QIGKNAMLRW GPFLYWTLLG VFHGLVFFFG VWFLFSNPAL QDNGQAFGNW SYGTIVFTIL
VFTVTLKLAL DTRHWTWINH FVIWGSLAFY VFFSFFWGGV IWPFLRQQRL YFVFANMLSS
VSAWLVIIVL ILLSLLPEIL YVVLRKPRGP YARQIAAVMP LSYKHLKERD
//
