ID Q551P7_DICDI Unreviewed; 1867 AA.
AC Q551P7;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=DDB_G0276541 {ECO:0000313|EMBL:EAL69224.1};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL69224.1, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL69224.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL69224.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=12097910; DOI=10.1038/nature00847;
RG Dictyostelium Genome Sequencing Consortium;
RA Glockner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000313|EMBL:EAL69224.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL69224.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL69224.1}.
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DR EMBL; AAFI02000015; EAL69224.1; -; Genomic_DNA.
DR RefSeq; XP_643097.1; XM_638005.1.
DR AlphaFoldDB; Q551P7; -.
DR SMR; Q551P7; -.
DR STRING; 44689.Q551P7; -.
DR PaxDb; 44689-DDB0237679; -.
DR GeneID; 8620501; -.
DR KEGG; ddi:DDB_G0276541; -.
DR dictyBase; DDB_G0276541; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q551P7; -.
DR OMA; GPNNDIY; -.
DR PhylomeDB; Q551P7; -.
DR Reactome; R-DDI-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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:SF218; P-TYPE PHOSPHOLIPID TRANSPORTER; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 363..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1662..1682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1712..1733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1745..1766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1778..1798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1818..1844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 633..685
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1598..1839
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 128..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1867 AA; 210703 MW; 1EA1D2810008D3C9 CRC64;
MSNYNGDYHY NNEQQQQNHH QQYRSTTDNS AILNGGVSYD LLDSTNSARS NNPLLQGMGY
EEDTFEEQQQ QEIYSNNDNS GNNNSNNNNG ASDKSYFTIY GNINNDAHNQ TLTQHTDLEH
VDLESDSKNI KYQQQQQQHQ HQQHQQYQQQ HQQHQQQNNN NNNNGYINPH LTESSQLFSS
VPLNSLPNSP YHINYPYTNN NSNSNNSYNN TNSNNNNNGN DVYSENNNSN NNNNNSNNKK
KYKKKSKRNI FKKKQDKESD LNKSNTPIII KDNDDDDDNN NNNNEDNNDD NQRNSKVFIH
KQHQSQVPDQ YLAILKASHS AVQRKKRDAI ALRVGRQWLT HIITVQTVGN LIRALPIFVL
EKYYVMLLIF FQGKIIYIYL TNKQTNKQTN KQTNKQTNNK QTDRQTEINR ALFLVIGSYG
VKRLKPYLIL LYVIGCFSTT ILDLIMTFTY AHTQSSRPFT EELLAFWSYV LFVSLLCILN
IIGGILLGLK LFVSVVSLQD PSDNSLILLT ASLVGSFDIE RDESASSSSS QAKASRCIFF
YGSDVKKAIA TTTSITKKLT TGEKIKQYFK LKKLFPKSPF SSGHNNNNYN NNDNNIINNN
NNNNGLNNNH NNNNNEQITS SVATSTDKSQ LLSMKTNQVI TSKYNVFTFI PKVIFYQFSR
LANLYTLAIV ILCMFSFSPV GPVSSLTPLL VVIAVTSFKE LAEDLKRHKQ DKEINGRETS
IYRPPFYIIS PTASKEDLKR RQSGFNGFIS RIGNFFGSIK QQYIQTEKNI PMVPDNDYSK
VGVFQSCHWE DIKVGDIIYV KNGESLPADI ICLSSSRSDG RAYLETANLD GETNLKAKSS
ISKCQWIKGA KDLDDFSCKV DYEGPNNDIY SFDGVLTILK GFERSNIGDS TVVPTTNYVP
VSIDQLLLRG TKLRNTDWVI GVVTYSGVDT KIEKNASKAS QKRSSVERGV NNKLLILFLL
QTIICIICSI GHNRWHLEDD KDAKPWYIDY DPEQTEDFIY VSYVILYNTL IPLSMYVSME
MIRVSNAHFI DSDLEMYDES TDTPAQARNT NINEELGQIQ YLFSDKTGTL TCNEMVFNRC
TIGGQVYGPE DSSLQDLRLF IKNQLSDSSN GSYLRQSNGL SGGGSGSGGS GGSGGDASSS
LNPLGIPVQP EISIPILSDQ TEYIKEFLTC LAICNTVLIE KNKEIDDLMM NHDNSKSHHN
FNGGTNSGCS VIPKYQAASP DEESLTLTAA RYGFILKSRE DNIITISVHG REERFELLNV
LEFNSYRKRM SVIVKNQKNQ IKIYCKGADS VIFERAKKNT DHCVGILQST EKHLSEFACS
GLRTLCMSVR TIEHEEYIAW NKIHQEASIS LVKKAEKVDA ACELIEKDLL LIGSTGIEDR
LQDHVPETIS ALREAGIKVW VLTGDKQETA ISISTSSAVI NEEMELIILN ESNKQALMKR
LLTISNEKRL HHFNDMSGRW GSVKYLSKLL EKVASKLRLE PSDAPNLLNK SNGMSAPAVN
ASQKHIAIII DGSTLALALE PDLRYFFLQV AKTCESVVCC RCSPSQKAKV VNLVAERSFL
FGDGAITMSI GDGANDVPMI QKAHVGVGIS GREGMQAVLA SDFAIANFSM LRRLILVHGN
RSYKRMTKLI LYSFSKNIAL SISQFWFGFF SGFSGQMIYF DFLFTLYNAL FTSLPVIFLG
TFDQDTKEDD LLNKPYLYRV CQSNSPFSTW KFIWWVFIGM WQSATIFFVT FFVMNTSTIE
GGKTLGLWSI GTAAYIYLVV TVNLQISFIT RYWTRQTILA VSISVVSTFL FVMLYSVLGR
YVEADATHII FELYALPTFW LLLIIAPSIA LLPYIIVSLN SWLFNTDNLS LQKLNLEKKG
FIMMNDL
//
