ID D8LGJ4_ECTSI Unreviewed; 1381 AA.
AC D8LGJ4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Esi_0168_0050 {ECO:0000313|EMBL:CBN79051.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN79051.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN79051.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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; FN648201; CBN79051.1; -; Genomic_DNA.
DR STRING; 2880.D8LGJ4; -.
DR EnsemblProtists; CBN79051; CBN79051; Esi_0168_0050.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; D8LGJ4; -.
DR OMA; MHSFWSW; -.
DR OrthoDB; 48945at2759; -.
DR Proteomes; UP000002630; Chromosome LG04.
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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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:SF150; 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; 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 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:UP000002630};
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 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1070
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1085..1106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1118..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1157..1175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 30..73
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 935..1185
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 236..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 151390 MW; 4B52095392BCEA31 CRC64;
MGAILTRPEI KPFRTIDILR EGVIGGQEQS AMADNSVVTS KYNVITFVPR SLFEQFRRIA
NVYFLVISVL MMLGWYTDLF ESPLAPFSTI IPLILVLSVT MVKDGAEDLK RHRSDNRVNN
TEATAMDIHT RGGFVPVAWK DVKVGMIVKI ADKEEIPADV VLLSSSEPGG VAYIETANID
GETNLKIRTS APTRPGQPPG PLWSSAEELH GVRMELEYEA PNARIHFFTG TLTLHGGAGG
PQDDSGEGGG GGTGSRDVPV DQSNLLLRGA RLRNTKWAIG VVAYTGRESK IAQNARSVPS
KQSNLDKVTN KIMFVIFTCM AVVTTLSLVG YLVFEAENDD KLYYLCYDSD NSPVPLFRDN
CESSDSSSSV GQWFTFLILY NNFVPISLYV TLEMVNFIQA AFIDEDILMY DETQDTPAQA
RSSNMGADLG QVEYVFSDKT GTLTQNLMKF KRCSVGGVIY GELDQKSKDL MTPQQLTHAV
DAPPLSELAS NIAGAEKGSA PLDFALCLAL NHTVVLEEDP KTGQKQMQAE SPDEEALVDG
GKTLGVNFVD RSPGKVELDV TGKGRLSYNL ILTIPFDSTR KRMSVVVRAP DGSYVLYCKG
ADNIIMDRSR GYMGSDKETV ASHLGVFSND GLRTLLLAKK EMSQEFFDEW YEKYRKASIA
TGDRAEQIAE VAKEVEADLD VVGATAIEDK LQDEVPATIA DLGKAGVKLW VLTGDKMETA
INIGYSCRLL EPEMTLIKLK EKEGDPQSVV NQLRALMTHF NRLVEDDGLV KRFWGHVKQS
PLGLLRRSRR HGGGGGLSAP SSMGDRNRTG GVATMEEDGA ATLPTPLLEQ PQGAPPLSEL
TADSLALVLD GPSLAHVLGN PEAERMLLTL GSMCKSVIAC RVSPAQKRLI VRLVKRGVVP
TPVTLSIGDG ANDVGMIQEA QIGVGISGKE GRQAVNNSDF AIAQFRFLKR LMLVHGHWDY
RRVCKVILYS FYKNFVLTFC LFYFCFYTGF SGQSLFESLV YSGFNFFTAM PILLIGIFDK
DVGNQTATEC HKLYAVGRAG MDLNLRTMTK WVCQAILDSL TVFFLPLAAY RDATTVWAER
GYGDGLYVFG TTVYAGLIMA MMMKVFNMTN TWNYQSWFFW WGSIALFFSF ISLYSLLVSY
AYDFYYVAMQ LMSRSAFWLI IIQVPCVTWS LDTLIKMLEH NFRPTVGHHA REFDRGFTSE
TGLQRLDEIK ARARAEELSP TPGGYTDVQE VLGPKRDDAN HKWKMGPETL RALNEGVNPG
ELASMGITAG SDAVPNRSSF AFDHVTADFG PGASAAQEEL RNLVAEEGEA HVRQSRSRSL
ERWDSASMSV AATTYGDTAA EGAAGGSTRR FLAAQDSAAG SVFAGSFRAG GGGVGEEKGR
G
//
