ID A0A168PE76_ABSGL Unreviewed; 1427 AA.
AC A0A168PE76;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ABSGL_08006.1 scaffold 9429 {ECO:0000313|EMBL:SAM02235.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM02235.1};
RN [1] {ECO:0000313|EMBL:SAM02235.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02235.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
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 EMBL; LT553750; SAM02235.1; -; Genomic_DNA.
DR STRING; 4829.A0A168PE76; -.
DR InParanoid; A0A168PE76; -.
DR OMA; WSYFIVL; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
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:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 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|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|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
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 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 553..572
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 584..605
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1167..1187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1199..1220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1248..1274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1286..1308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1314..1334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1354..1377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 75..129
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1136..1382
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 20..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 160624 MW; FF42C76745E7F4CF CRC64;
MAALNPKSFL RRKARFFTTT DDNDDDNDND NDSDNNTRNL RRTESTSSYM QRRRNIYVNM
DLPASEYDEK GQPIDRHYVS NRIRTAKYTI LSFVPKNLFE QFRNVANLYF LFLVILQCIP
LFGVTEPAVS ALPLIAILVI TGIKDAFEDW KRNQSDQRVN NATTRTLHNW KNVNTPIATR
GSFFPLFVFL GFFCALAGVE NRFTQCYRLA QLPKQPKNIV FSDGQLDNND TSPTVAFSSD
DSPLPPPPKL IDPVDQPVVT EPRRLLTTVR QRSDTLRSEL SSMFKPKRQP YRPGNIPHSV
LYRTATNDTS NANATQTSLP ENPEDQSLFG GRRPSHHNLT RMPTGGGGCV HSNCDTKWKD
IRWQDLHVGD YVQIRNDEDV PADVVVLSTS EPDSICYIET QNLDGETNLK VRQGLEGTSD
IQTEHDCEQA SFYIESEPPH VNIYQYNAVM RWTIDPKDTG TMRSGVSHEK SDAISYNNIL
LRGCVLRNTE WVIGIVVYTG NDTKIMLNSG QTPSKRSKMA KATNPHKVKK LGKGGGTHGI
LAGGIHGYLA GGIHGYLAVT LYTLWGVLAL YVKGVTMSNS YSSAFFRVTL ILYQNIVPIS
LYISIELVKS VAAYFIHSDI DLYHEETDTP CIPKTWNISD DLGQIEYVFS DKTGTLTQNV
MEYRKCTIDG ISYGLGKTEA QMGAVKRVNE PIKKADGTGA LNLDLEDHET GVTLDANNTA
AAEVDDLADA RKEMFDKQAQ LFKNTHIGPN PTFVDPQLFD DLAKNDPHAH AVQHFLLTLA
LCHTVIAERP DPENPDTIEY KAQSPDEAAL VATARDLGFV FLGRDANTVH AEIKGERKSF
DVLNTLEFNS TRKRMSVIIR PHDSDKIVLL CKGADSVIFE RLCNDFGPQE DLQKAQLDLR
DTTLAHLEDY ANEGLRTLCL AYRFIASEDY LPWQRRFQEA SSSIVNREER VDAVSEEIEK
NMLLMGGTAI EDRLQDGVPE TIAELAKSGI KLWVLTGDKT ETAINIGFAC NLLTTDMELI
VLKASNREET KDQLVEALEQ SDSDNKDNLA LVIDGTTLKY GLEPETKEMV LSLGMRCKSV
ICCRVSPKQK AQVVNMVKKG LKVMTLAIGD GANDVSMIQE ANVGIGISGV EGRQAVMASD
YAIAQFRFLR KLLLVHGRWS YIRTAEMIMG FFFKNIVWTF ILFWYQFFCQ FNGTMVFDYS
LVTLYNLVFT SLPIAFLGIW DQDLDSETSL LYPELYRMGL RNDKFKKWQF WVAVFDSIYQ
SAVCFFFPYM LLVAGGADST GHDANGVYEI GTIVSGICVC VANFYVSFSL YSHTWIQFMI
ISLSILVYFA FIGIYSQFNT FIFAGHVRLF GPGLYWLVLI LTVVAAFIPR LVLSYVLHQY
YPYDNDIIRE TELVLKRGNH GNADVNVDHH LNSAQDIKLQ DRRSISA
//
