ID A0A2K5DUB6_AOTNA Unreviewed; 1222 AA.
AC A0A2K5DUB6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B2 {ECO:0000313|Ensembl:ENSANAP00000024541.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000024541.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000024541.1}
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 RefSeq; XP_012331741.1; XM_012476318.1.
DR AlphaFoldDB; A0A2K5DUB6; -.
DR Ensembl; ENSANAT00000042460.1; ENSANAP00000024541.1; ENSANAG00000029979.1.
DR GeneTree; ENSGT00940000160804; -.
DR Proteomes; UP000233020; 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; 1.
DR PANTHER; PTHR24092:SF46; PHOSPHOLIPID-TRANSPORTING ATPASE ID; 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; 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000233020};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 350..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 903..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1025..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1055..1076
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1096..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 49..114
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 872..1125
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1194..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 138655 MW; F691BF5207854485 CRC64;
MDTLRAVPLF SISGLFFSHR VSHGIAGTLL GEMALCAKKR PPEEERRARA NDREYNEKFQ
YASNCIKTSK YNILTFLPVN LFEQFQEVAN TYFLFLLILQ LIPQISSLSW FTTIVPLVLV
LTITAVKDAT DDYFRHKSDN QVNNRQSQVL INGILQQEQW MNVCVGDIIK LENNQFVAAD
LLLLSSSEPH GLCYIETAEL DGETNMKVRQ AIPVTSELGD ISKLAKFDGE VICEPPNNKL
DKFSGTLYWK ENKFPLSNQN MLLRGCVLRN TEWCFGLVIF AGPDTKLMQN SGRTKFKRTS
IDRLMNTLVL WIFGFLVCMG VILAIGNAIW EHEVGTRFQV YLPWDEAVDS AFFSGFLSFW
SYIIILNTVV PISLYVSVEV IRLGHSYFIN WDKKMFCMKK RTPAEARTTT LNEELGQVEY
IFSDKTGTLT QNIMVFNKCS IYGRSYGDVF DVLGHKAELG EKPEPVDFSF NPLADKKFLF
WDPSLLEAVK IGDPHTHEFF RLLSLCHTVM SEEKNEGELY YKAQSPDEGA LVTAARNFGF
VFRSRTPKTI TVHEMGTAIT YQLLAILDFN NIRKRMSVIV RNPEGKIRLY CKGADTILLD
RLHQSTQELL NTTMDHLNEY AGEGLRTLVL AYRDLDEEYY EEWAERRLQA SLAQDSREDR
LASIYEEVEN NMMLLGATAI EDKLQQGVPE TIALLTLANI KIWVLTGDKQ ETAVNIGYSC
KMLTDDMTEV FIVTGHTVLE VREELRKARE KMMDSSRSVG NGFTYQEKLS SSKLTSVLEA
VAGEYALVIN GHSLAHALEA DMELEFLETA CACKAVICCR VTPLQKAQVV ELVKKYKKAV
TLAIGDGAND VSMIKTAHIG VGISGQEGIQ AVLASDYSFS QFKFLQRLLL VHGRWSYLRM
CKFLCYFFYK NFAFTMVHFW FGFFCGFSAQ TVYDQYFITL YNIVYTSLPV LAMGVFDQDV
PEQRSMEYPK LYEPGQLNLL FNKREFFICI AQGIYTSVLM FFIPYGVFAE ATRDDGTQLA
DYQSFAVTVA TSLVIVVSVQ IGLDTGYWTA INHFFIWGSL AVYFAILFAM HSNGLFDMFP
NQFRFVGNAQ NTLAQPTVWL TIVLTTVVCI MPVVAFRFLR LNLKPDLSDT VRYTQLVRKK
QKAQHRCMRR VGRTGSRRSG YAFSHQEGFG ELIMSGKNMR LSSLALSSFT TRSSSSWIES
LRRKKSDSAS SPSGGADKPL KG
//
