ID A0A0X8HUL3_9SACH Unreviewed; 1592 AA.
AC A0A0X8HUL3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=AW171_hschr63684 {ECO:0000313|EMBL:AMD21714.1};
OS Eremothecium sinecaudum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD21714.1, ECO:0000313|Proteomes:UP000243052};
RN [1] {ECO:0000313|EMBL:AMD21714.1, ECO:0000313|Proteomes:UP000243052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD21714.1,
RC ECO:0000313|Proteomes:UP000243052};
RA Dietrich F.S.;
RT "Genome sequence of the yeast Holleya sinecauda.";
RL Submitted (JAN-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; CP014246; AMD21714.1; -; Genomic_DNA.
DR RefSeq; XP_017988710.1; XM_018133164.1.
DR STRING; 45286.A0A0X8HUL3; -.
DR GeneID; 28725018; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000243052; Chromosome vi.
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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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 Translocase {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 402..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 447..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1337..1354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1366..1391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1411..1434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 115..172
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1191..1441
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 891..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1592 AA; 180734 MW; 858E7122AD6BABC5 CRC64;
MGNRRRSKSL RTQLFNRNLY DQWKQQENVE GIGNETGGIP LGDIPESQAV DNNAIAKTKG
DDIWSRIAGK LFCKACNDRE RKGRTIPLCL CKRRRLDEKL ERLYDSSRVL LDERTNKPYV
KNDITSSRYT IYSFLPRQLY AQFSKLANAF FYCIALLQMV PTWSTTGNYT TIIPLSIFMS
ISIAREGWDD YKRHKLDKVE NDRLVKVLVV DVEDSECGSA TLNSKLGENK SFADEALLQS
YGVSIVQKPW KSISVGDFIL LNQDDWVPAD LMLLTADGEN DCVYVETMAL DGETNLKCKQ
PVPDISSRMR SAEGLINFTA SVTVEDPDNN LYNFDGNVEF TNSNKEKKMV PIGLDNVVFR
GSIVRNTNAL VGMVVFTGEE TKIRMNSIKN PRIKAPKLQT RANWIVLFLI IVVVSLAVLS
LGLQRYYKRR YVDNNNAWYL WGQDAGIVAS LVSYIIMYNT MIPLSLYVTM EIIKTMQSRL
MMWDIDMYHP ESNTPFQSRT NTILEELGQV SYIFSDKTGT LTENKMVLKR FSICGSSWTH
EVENGENGFQ KSAASNDVDV ISVEDDNSIG KNFEITEPEP RTSVECKGTS SVTYSGRPSI
ASQIEKLKFE ISGARKKEEN NYLSSVPSVN ATVTSSESRL KSTSDLILYV QSHPRTFFAQ
RVKMFMLSLA LCHTCLPKKV SDDADDADSI EYQASSPDEL ALVMAARDMG FVFLNRNTNI
FTIKTFPNGF EKEPLLEDYE ILDVIEFNST RKRMSVLVRV PNVQDKVLLI CKGADNVILE
RLQNSEMALE KTREINISTT RRKTEEADLV LQHRRQSMDQ ISRRDSIGDI LRNSISGRPT
RGSWAVQAAS SSYAINPTRS LTDQELHINS IDDFLNIGTK ADEEADHLYN ASRKSLSKQQ
REKYSRKVGE KGSSPVQVKK SEQGLPKAEY SEKRDSLESY IGSDELVQNE EYVLERTLYD
IDSFSTEGLR TLLYSFKWVS QQEYQTWSAR YQVAKTSIVD RRELMDSVGG SIEFGLRILG
VSAIEDKLQE GVSEAIVKLR RAGIKLWMLT GDKRETAINI GYSCKLIRDY SSVVVLSSHA
DDMTSKITAL IQQLDEGNVA HCVVVIDGAT LATFEENPIL MALFVELCTK TDSVICCRAS
PAQKALMVEN IRKTDKKIVT LAVGDGANDI AMIQSADIGI GITGKEGLQA ARSSDYSISQ
FRYLLKLLLV HGRYNYIRTT KFMLCTFYKE LIFFIAQQIY QRNVMFSGTS LYEPWSLTMF
NTLFTSLTVL CIGMFEKDLK PMTLLAVPEL YSLGRLSQAF NMFMFLRWML AAAANSVLIC
FLSWYCWGFT SLSDNTLYPM GTIIYTAIVI LINVKFQFLE MNSRTWLAFG SVFISIIAWF
LWCSMLPKIY RQNFSTYDVK DMLYHTIPKD YTFWLTIVIA VALPLILNIV FLTLRTMLWP
TDSNIFYELE HQDAIRKKLE LNAFNELKQG WTWQRDPPAF FRWSKKILGH SKENSSVVSN
SSLSIKHTGS EPNESALDTP KATALENNAA FDSDEFEQLP SGKLIKRKKQ GPNGSHENLN
EGLTARIGRK LRLKSKDEDI NEIINQRLRS LE
//
