ID A0A3B4G323_9CICH Unreviewed; 1124 AA.
AC A0A3B4G323;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:ENSPNYP00000017277.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000017277.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000017277.1}
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}.
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DR AlphaFoldDB; A0A3B4G323; -.
DR Ensembl; ENSPNYT00000017709.1; ENSPNYP00000017277.1; ENSPNYG00000012883.1.
DR GeneTree; ENSGT00940000158878; -.
DR Proteomes; UP000261460; 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 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 286..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 967..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1004..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1035..1056
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1076..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 39..92
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 853..1100
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1124 AA; 128737 MW; 0901913F40EE432B CRC64;
MCSHGLLFFS TQRRINRLGS RTIYVGHRPC PANEVFIPPK FCDNRIVSSK YTVWNFLPKN
LFEQFRRIAN FYFLIIFLVQ VIVDTPTSPV TSGLPLFFVI TVTAIKQGYE DWLRHKADNE
VNKYRVTVLE DGRRIQKESE KIKVGDVLEV EEDETFPCDL ILLQSSRDDG TCFVTTASLD
GESNHKTHYT VPDTERDVES LNATIECEQP QPDLYKFVGR MHIYKNNEEP SLRSLGPENL
LLKGATLKNT QSICGVAVYT GMETKMALNY QGKSQKRSVV EKSINAFLLV YLCILVSKAL
VCTTLKYVWQ SKPGQDEPWY NEKTLKEKET NLYLNMFTDF LSFMVLFNFI IPVSMYVTVE
MQKFLGSFFI SWDKDFFDSE IEEGALVNTS DLNEELGQVE YVFTDKTGTL TQNNMEFIEC
CIDGHQYKYR DASSEVDGFC VTDGPMNTVQ QKAGREREEL FLRALCLCHT VQVKESTEQG
QGQDGRIDQV DGLMVDGQVV PPLQEQRGFI ASSPDEIALV QGAMRYGFTF LGLESKTMKI
LNRANDVEMY ELLHVLNFDP VRRRMSVIVR SISGETLLFC KGADSSIFPR VKQEEVEKIR
MHVERNATDG YRTLCVAYKH LTAEEYDQVD SGLREARLAL QDREEKLMAV YNQVETGMNL
IGATAVEDRL QEEAAETMEA LQGAGIKVWV LTGDKMETAK STCYACRLFK RNTELLELTV
RTLESPGKRR EDRLHDLLLE YHKKTVQDAP PITKVCDYGF IVDGATLSMV LNSSSENNLH
DYKDLFLQIC QNCTSVLCCR MAPLQKAQIV KMVKNSKGSP ITLSIGDGAN DVSMILEAHV
GIGIKGKEGR QAVRNSDYAI PKLKHLKKLL LGHGHLYYVR IAHLVQYFFY KNLCFILPQF
LYQFFCGCSQ QPLYDAAYLT MYNICFTSMP ILAYSLFEQH ISIEMLLENA TLYRQIGKNA
MLRWGPFLYW TLLGVFHGLV FFFGVWFLFS NPALQDNGQA FGNWSYGTIV FTILVFTVTL
KLALDTRHWT WINHFVIWGS LAFYVFFSFF WGGVIWPFLR QQRLYFVFAN MLSSVSAWLV
IIVLILLSLL PEILYVVLRK PRGPYARQIA AVMPLSYKHL KERD
//