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Database: UniProt
Entry: D7FU18_ECTSI
LinkDB: D7FU18_ECTSI
Original site: D7FU18_ECTSI 
ID   D7FU18_ECTSI            Unreviewed;      1755 AA.
AC   D7FU18;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Phospholipid-transporting ATPase, putative {ECO:0000313|EMBL:CBJ31545.1};
GN   ORFNames=Esi_0263_0021 {ECO:0000313|EMBL:CBJ31545.1};
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:CBJ31545.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ31545.1, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FN648446; CBJ31545.1; -; Genomic_DNA.
DR   STRING; 2880.D7FU18; -.
DR   EnsemblProtists; CBJ31545; CBJ31545; Esi_0263_0021.
DR   eggNOG; KOG0206; Eukaryota.
DR   InParanoid; D7FU18; -.
DR   OrthoDB; 103847at2759; -.
DR   Proteomes; UP000002630; Unplaced LGUn.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1187..1205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1226..1246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1261..1279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1309..1330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1342..1360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1372..1396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1402..1428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..59
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1098..1151
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|Pfam:PF00063"
FT   DOMAIN          1195..1443
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          475..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1508..1530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1557..1596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1611..1635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1657..1704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          859..893
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        478..504
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..549
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1516..1530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1664..1685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1755 AA;  192641 MW;  0F50C73A75936A32 CRC64;
     MLDMRYLHAF AGYTHWDFLP RFLMEEFHPR RKMANAYFLV LASLQTIPEI TNTFRVPTIL
     LPLSVVVIVD AVFAILEDVG RHPANPKGNA SPTRALDVDL QRSAGKFPRV EWRDVQVMGA
     HEPNPQAKAG ICYVETKSLD GETNLKIRQA IRSTIGRVST PRDAAALKGR VVMEHPNKLI
     DNFSGTIEVE GAGDDGGSCR EVIQTRNLLL RGCVLRNTRW VVGLVLNTGP DTKIVMSSLE
     PPHKTSRLEQ RTNVEVWRIV RLLCLVCFLG AVGSLVWNAT SAEDHVYLRI DVGSWGNQMK
     TTFIQFLYLF LLLGNFIPVS LYVSMGTVKF SQAFFMKQDL DMYHEDTDTP ALVRTMALNE
     ELGQVSHVFS DKTGTLTQNV MDFRKFSVGG VSYGRGVTTI ARAVAAELGH EIPQEDLEAE
     AVIAKQPPVP HVRFYDPRLL EDLQSSTGEE QRALLLDFFL ALAVCHTVIP ERGLSSRSGR
     RRRCRGPGGG SRHPHRSRSR ERRRTNKPVG REQSRQTRYS SGARTGDFVQ DGEEEEEEEV
     VAEQREQEEQ EEEGPAKLSA SSPDDEALVL GARHFGMEFR DRLDNKACVR RSGPFLRGQQ
     QHHQQHPLRS PPAPGEKPKG EEGRDGRGFA TGGEGGWPQV AEQGSRPGGD RFVDEKYEVL
     RILDFTSARK RMSVIVRAPD GRVRILCKGA DSVMIPRLAR NSSASDSSAG DSVPDDHHHH
     LDASNPLPFG AAFGPAATAI PAPTTVAPAP APGGKTLPAA SPQEGAAQAV SPASDAAVNA
     AAAVRLPLAD VVAEECGGGG GGLAGNWSTS SEDNRPGGER SEERTLKHME TYAREGLRTL
     LVTCADLDGD WFRAWDKRFE TASTDLSEVE KKKQGLENEI DRLMNEVEKN LRLLGCTAIE
     DKLQDGVGTC VDALQRARVK VWMLTGDKEE TAINIGVACQ LLGPEEQMER IIVNMDPQTG
     CQDVEEVKDR LEDELNRISD EDPFHKSRGK GSGGTGDGGT GEDGGGVPRK GGRQRALIID
     GQALSLAMDP ACSKYFAELA MECEAVVCCR VSPDQKRAVV ALVRERRPEA RTLAIGDGAN
     DVAMIQAAHI GVGISGQEGM QSVGAQFKNQ LNSLLGAIGE THPHYVRCLK PNDENVRSQF
     DLGRITAQLA NGAVAAKARR EAALRDKRCR QRGGGIYGRH RPVCCRTLLY VPLAVNASDF
     AIAQFRFLQK LMLFHGRQNY RRMSKLVAYT FYKNILMAVP MAWYMVVNGY SGQKFYTEGG
     IQFYNIMFTL WPILFLGCFD RDVSLKDTEN FPQLYVLGIN DVFFNAKVFW SWMSQAIVEA
     ALITFVPLLL LKGGPADDGA EVSYMFYGGT TFSLVVLLAN SKILWLQYRW TWWAAVLVMA
     SVLAWFGTAC VLNILHKVDF DFFMVFFHLM VNPTFWAVVT LCFTAVAMRD LSWKFYHRWW
     QPKLHHLILE VEASRGDPVI LTDSGTPEVG GGGAGFGVGV ADSRRKSWER RGKRAGDGLG
     GRAVAVQGEG GATAAGRDDD GFEKQARRED KASAVLSPAF SDAVELCLGG EDAGDAVAER
     PRGGREEVLG GRAGASYGGG GGGGGRGFRR GHSHDDDEGY AAVYRRLTDA LSSQPSTGNG
     GGEGTSVTPA TSHCPSVSST LPLELIFPAV AAQGPVAMGR SRSDQLPKRS SSSRRLQQSP
     HQSGAVGTRF PRAPSGGFAY STDEDSASME SRMILNYVES PLKKTPEFWE APRPVLDRLN
     RRRERGKFCW RWCRC
//
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