ID A0A1E3NID7_9ASCO Unreviewed; 1150 AA.
AC A0A1E3NID7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PICMEDRAFT_35360 {ECO:0000313|EMBL:ODQ45846.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ45846.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ45846.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ45846.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454004; ODQ45846.1; -; Genomic_DNA.
DR RefSeq; XP_019016959.1; XM_019162937.1.
DR AlphaFoldDB; A0A1E3NID7; -.
DR STRING; 763406.A0A1E3NID7; -.
DR GeneID; 30179624; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000094455; 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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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:SF214; 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; 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|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:UP000094455};
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 299..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 341..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 899..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 942..964
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 976..995
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1007..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1041..1065
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 38..104
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 829..1079
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1150 AA; 130313 MW; 3D8883826A043AD3 CRC64;
MHDHRPPPEV VNTEKNIFDI RRCWSKRKNE DDKGPRVIYL NDPHKNSKSG FSLNHISTTK
YNAFTFLPKF LFEQFSKYAN LFFLFTSCIQ QVPTVTPTNR YTTIGTLLIV LLVSAVKEMS
EDIKRSSSDN ELNKSKVLIL DSTTGEYHEK KWINVNVGDI VKIRNGDSLP ADLILLSSSE
PDGLCYIETA NLDGETNLKI KQPRKETVHL IDPHKLVEVK GKILSERPNS SLYTYEGTME
LNNTQFALSP DQLILRGASL RNTMWIQGVV IFTGHQTKLM RNATATPIKR TDVERIINLQ
IIALFGILIF LAIVSSLGNV LTLQINRKHL SYLYMEGTSK VGLFFLDILT YWILYSNLVP
ISLFVTVEII KYYQAYLIAS DLDMYCEEND TPTVVRTSSL VEELGQIKYV FSDKTGTLTR
NIMEFKTCSI GGRCYIENIP EDKEAVMQDG VEMGYFTFDQ LKKDLTSGSN SKVIDSFLTL
LSTCHTVIPE VGEDGTIKYQ AASPDEGALV DGAAMLGYKF HTRKPSSIVV SANGQDLTFE
LLNICEFNST RKRMSTLFRC PDGKIRLYVK GADTVIFERL ASDNEYVEAT TKHLEEFAVE
GLRTLCIAAR VITEEEYVSW SKVYQQASVS LENRAEELDK AAELIEKDLF LLGATAIEDK
LQDGVPETIS VLQEAGINVW VLTGDRQETA INVGMSCKLL SEDMNLLVIN EENKNDTCEN
MIEKLTVLHG EEISKEDRDS LALIIDGKSL GYALEPDLED MFLEIGTMCK AVICCRVSPL
QKALVVKLVK RKKKALLLAI GDGANDVSMI QAAHVGVGIS GMEGAQASRS ADFAIGQFKY
LRKLLLVHGA WSYQRISLAI LYSFYKNITL YMCQFWYVFS NGFSGQSIVE SWSLTLYNVL
FVALPPFVIG IFDQYLTINM LYQYPQLYKI GQQGHFFNVE IFWSWAVNGF YHSAIIYVCV
INIYKYGNQF LDGQIGGLWV VGVAIYSVCL LTSLGKAALV SSQWTKFTLI AIPGSFALWF
IAFPLYAVIA PKANVSKEYR GIVPFVYGSG VFWLTIIVVP ILCLMRDFLY KFYKRQWNPE
FYHIVQKVQK SQIQTHRPKF SSFQKTIRKV RQVHRMRKQR GFAFSQVEGQ ENIVRKYDTT
KRRGVYGELE
//
