ID F0ZVN9_DICPU Unreviewed; 1183 AA.
AC F0ZVN9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=DICPUDRAFT_49853 {ECO:0000313|EMBL:EGC31992.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC31992.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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 -!- 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; GL871218; EGC31992.1; -; Genomic_DNA.
DR RefSeq; XP_003291490.1; XM_003291442.1.
DR AlphaFoldDB; F0ZVN9; -.
DR STRING; 5786.F0ZVN9; -.
DR EnsemblProtists; EGC31992; EGC31992; DICPUDRAFT_49853.
DR GeneID; 10507658; -.
DR KEGG; dpp:DICPUDRAFT_49853; -.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; F0ZVN9; -.
DR OMA; MHSFWSW; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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; PF00122; E1-E2_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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001064};
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 335..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 927..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1003..1027
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1047..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1117..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 74..140
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 897..1146
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 779..806
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1183 AA; 134588 MW; F42831E3867F3172 CRC64;
MMNSSSTNSF RPYNGNVEIP LQDLQNGANS NSNLNGAYMN SMDNDDDYEG GFVQKVQNFI
LRIRDDFIGN CRTIHINNHE YNLLYKYTNN YVKTSKYSLV TFVPLNLFEQ FCRLANFYFL
IVSCLQLIPG VSPTGRFTTL GPLCIVLTVT ALKEAYEDYK RHKEDDRVNY STTEVLRNSS
FVHVLWKDIQ VGDIIKVYDK QFMPADILLL STSEPDSTCF VETANLDGET NLKMKQSLEE
TQFLADDLNQ LSSFNGLIEC EHPNKRLYSF SGSLLMEQKV LPISIKQVLL RGTMLRNTKW
INGLVLYSGR DTKLMRNSNT TPLKRSQIEK STNHYIIFIF FLQMLLCTAC AIANGSWTAS
NRKAFYLSFT RSNAVEGGMS FLTFLILFNN VIPISLYVTM EIVKLIQAYL INNDAEMYHK
ETDTPALART SNLNEELGQI EYLFTDKTGT LTQNKMIFKK CSIGGIVYGN ETNNNRSSSN
QSTPATPNVL NNLDDINNNN TNSSISSKLH KSNNSVNLQP VDFHDDKLLS DLNSKTDQSH
NIQEFLNIMA VCHTVVPEQE DGKINYQASS PDENALVNAA KFFGFEFTHR NQKNVFLKLN
GLEDIRFEVL QVLEFNSERK RMSVIVRSPN GKLLLYCKGA DSVIFERLAP NQPYADVTIN
HLQDFASEGL RTLCIAYCEL DQQVYQEWLK EYQIASTAII NREAEIDRVA EIIETNLFLL
GATAIEDKLQ KGVPEAINIL REAGIKLWVL TGDKQETAIN IGYSCQLLTP EMELVIINEQ
SKENTIVELN RRLNDLSTRS NSTENKEQMA LIVDGNTLNH ALEGHIKYSL LKLAKNCSAV
VCCRVSPSQK AQLVRLVKDN LASVTLAVGD GANDVSMIQA AHVGIGISGE EGLQACRSSD
YSIGQFRFLV RLLLVHGRYS YRRISKLVCY CFYKNIALYI TQFWFTIFNG WSGQTLYERY
TLTAYNVVWT FFPIIIMGIM EKDVSESILI EHPKLYQLGP KKILFSFPVF WGWVLNGIYH
SFVFFAIPAA ASYKSNAYSG GENSELFAFG LICFAAIIIT VNLKLALEVR YWTWVNHLAT
WGSMVVFFCW ILIYGRVNAK GIDSDLFDVI YRIGESAHFY FLLLLVPIIA LWRDFGWKFV
NRYYKPMPHH IAQELLKSND SKYVSKRTFS SYAFDTQELG QSD
//
