ID A0A1U8C9E9_MESAU Unreviewed; 1187 AA.
AC A0A1U8C9E9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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|RefSeq:XP_012976082.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012976082.1};
RN [1] {ECO:0000313|RefSeq:XP_012976082.1}
RP IDENTIFICATION.
RG RefSeq;
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_012976082.1; XM_013120628.2.
DR AlphaFoldDB; A0A1U8C9E9; -.
DR GeneID; 101843516; -.
DR CTD; 57198; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000189706; 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; 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:UP000189706};
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 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 315..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 868..889
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 951..970
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 990..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1020..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1061..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 49..79
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 837..1090
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 134425 MW; 1FC62C718E4E6618 CRC64;
MTVPKEMPEK WARAGAPPSW SQKKPSWGTE EERRARANDR EYNEKFQYAF QEVANTYFLF
LLILQLIPQI SSLSWFTTIV PLVLVLSITA VKDATDDYFR HKSDNQVNNR HSQVLINGVL
QQEQWMNVCV GDIIKLENNQ FVAADLLLLS SSEPHGLCYI ETAELDGETN MKVRQAIPVT
SELGDISKLA KFDGEVICEP PNNKLDKFSG TLYWKENKFP LSNQNMLLRG CVLRNTEWCF
GLVIFAGPDT KLMQNSGRTK FKRTSIDRLM NTLVLWIFGF LVCMGVILAI GNAIWEHEVG
TRFQVYLPWD EAVDSAFFSG FLSFWSYIII LNTVVPISLY VSVEVIRLGH SYFINWDKKM
FCMKKRTPAE ARTTTLNEEL GQVEYIFSDK TGTLTQNIMV FNKCSIHGHS YGDVFDVLGH
KAELGERPAP VDFSFNPLAD KKFLFWDPSL LEAVKMGDPH THEFFRLLSL CHTVMSEEKS
EGELYYKAQS PDEGALVTAA RNFGFVFRSR TPKTITVHEL GTAITYQLLA ILDFNNIRKR
MSVIVRNPEG KIRLYCKGAD TILLDRLHPS TQELLNSTTD HLNEYAGDGL RTLVLAYKDL
DEEYYEEWAR RRLQASLAQD SREDRLACIY EEVESDMMLL GATAIEDKLQ QGVPETIALL
TLANIKIWVL TGDKQETAVN IGYSCKMLTD DMTEVFIVTG HTVLEVREEL RKAREKMVDS
SHTVGNGFTY QGKLSSSKLT SVLEAVAGEY ALVINGHSLA HALEADMELE FLETACACKA
VICCRVTPLQ KAQVVELVKK YKKAVTLAIG DGANDVSMIK TAHIGVGISG QEGIQAVLAS
DYSFSQFKFL QRLLLVHGRW SYLRMCKFLC YFFYKNFAFT MVHFWFGFFC GFSAQTVYDQ
YFITLYNIVY TSLPVLAMGV FDQDVPEQRS MEYPKLYEPG QLNLLFNKRE FFICIAQGIY
TSVLMFFIPY GVFAEATRDD GTQLADYQSF AVTVATSLVI VVSVQIGLDT GYWTAINHFF
IWGSLAVYFA ILFAMHSNGL FDMFPNQFRF VGNAQNTLAQ PTVWLTIVLT TAVCIMPVVA
FRFLRLSLKP DLSDTVRYTQ LVRKKQKAQH RCMRRVGRTG SRRSGYAFSH QEGFGELIMS
GKNMRLSSLA LSGFSARSSS SWIESLRRKK SDSANSPGGG TEKPLKG
//
