ID A0A0D0V8J3_9TREE Unreviewed; 943 AA. AC A0A0D0V8J3; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 27-NOV-2024, entry version 44. DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033}; DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033}; GN ORFNames=I313_03119 {ECO:0000313|EMBL:KIR41165.1}; OS Cryptococcus deuterogattii Ram5. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus gattii species complex. OX NCBI_TaxID=1296110 {ECO:0000313|EMBL:KIR41165.1, ECO:0000313|Proteomes:UP000053392}; RN [1] {ECO:0000313|EMBL:KIR41165.1, ECO:0000313|Proteomes:UP000053392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ram5 {ECO:0000313|EMBL:KIR41165.1, RC ECO:0000313|Proteomes:UP000053392}; RG The Broad Institute Genomics Platform; RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D., RA Dromer F., Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Cryptococcus gattii Ram5."; RL Submitted (JAN-2015) 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 + phosphate CC + H(+); Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, CC ChEBI:CHEBI:456216; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KN847901; KIR41165.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0D0V8J3; -. DR HOGENOM; CLU_000846_6_0_1; -. DR Proteomes; UP000053392; Unassembled WGS sequence. DR GO; GO:0005768; C:endosome; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0005802; C:trans-Golgi network; IEA:TreeGrafter. 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:0006897; P:endocytosis; IEA:TreeGrafter. DR GO; GO:0045332; P:phospholipid translocation; IEA:TreeGrafter. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:TreeGrafter. DR FunFam; 3.40.1110.10:FF:000073; Phospholipid-transporting ATPase; 1. DR FunFam; 3.40.50.1000:FF:000009; Phospholipid-transporting ATPase; 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; 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:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 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 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|ARBA:ARBA00022842, 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:UP000053392}; 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 209..228 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 234..253 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 741..764 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 770..789 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 819..839 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 845..866 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 873..895 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT TRANSMEM 907..925 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362033" FT DOMAIN 707..934 FT /note="P-type ATPase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16212" FT REGION 25..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 335..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..57 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 943 AA; 104329 MW; D8C98443BCD81FC8 CRC64; MGKEAFDDYS RYLRDREANS TRYLVLVPQP PSPNPSSDRE QTPSLPRPQT RSTPASSIKV GDMVLLEKNQ RVPADMVLLT TSEEEGTCFI RTDQLDGETD WKLKVAVGET HKMGEAFVGN AEGSLYADPP IKDIHTFYGV FTLRSTSPGE QTETSTPLSV ENVLWANTVL AAGSAVGLVV YTGKETRAVL NTSEAGTKMG TLEKEVNKMA KILCTVTFAL SVFLVALNGF RGHWYIYVFR FLILFSSIIP ISLRVNLDMG KTVYAHQIQV DREIPETIVR TSTLPEELGR VEYLLSDKTG TLTRNEMELK KLHMGTLVFG WDSMDEVSHL LSQALDETSG PHGRQGSLPG GNQRGKRDMT GRVRDTVMAL ATCHNVTPVI NDDGTTTYQA SSPDEVAIVQ WTESVGLTLT SRDRTSMVVR TSAGRSLTFD ILSVFPFTSE SKRMGIIIKD RETGGVTFVQ KGADVVMSKI VHKNDWLEEE TGNMAREGLR TLVLGRKKLS EETYAAFDKA YRAAQLLPSE SRASSIASVI SQHLENELEL LALTGVEDKL QEDVKSTLEL LRNAGLKIWM LTGDKIETAT NIAVSSKLVA RGQYIHQVAK LRTADQVRDM LDFLHTKLDC ALVIDGESLQ LALDRFRSEF IILATQLPIV VACRCSPTQK ADVAKLIREF TKKTVCCIGD GGNDVSMIQA ADVGVGIVGK EGKQASLAAD FSINQFSYLT KLLLWHGRNS YKRSAKLSQF VIHRGLIIAV IQAVFSSIFF FAPIALYQGW LQVGYATLYT MAPVFSLVLD KDVNEDLALL YPELYKDLTK GRSLSYKTFF TWLTISVYQG GIIMLLSLLL FESEFLHIVA ISFTSLVINE LIMVALEVTT WHSYMVLSEL GTALVYFGSM AVLPAYFDLT FVLSSTFVYK VAVIVAVSSF PLYVIKAAHQ RLNPAAYKKV AGI //