ID A0A2K3D566_CHLRE Unreviewed; 1667 AA.
AC A0A2K3D566;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CHLRE_12g536050v5 {ECO:0000313|EMBL:PNW75666.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW75666.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW75666.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
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; CM008973; PNW75666.1; -; Genomic_DNA.
DR STRING; 3055.A0A2K3D566; -.
DR PaxDb; 3055-EDP03553; -.
DR EnsemblPlants; PNW75666; PNW75666; CHLRE_12g536050v5.
DR Gramene; PNW75666; PNW75666; CHLRE_12g536050v5.
DR InParanoid; A0A2K3D566; -.
DR OMA; IDVQWHE; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000006906; Chromosome 12.
DR ExpressionAtlas; A0A2K3D566; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; 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; 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:UP000006906};
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 378..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1027..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1054..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1096..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1170..1191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1211..1229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 30..85
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 987..1239
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1295..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1667 AA; 177160 MW; E8C5CFF3E11169EF CRC64;
MGLFRRADGP AVVAEAHRHI PLGSSLDTEE HLPYRGNYAS TTKYTLLTYL PKALFEQYRR
VANIFFTLMA ALSLTPFSPL RPWTCWTPLV LVVGVSMIKE AREDYKRYKQ DREVNERPTR
VLDRKTGEFV TIPWKALRVG DIVQVCRDEY LPADLVLLST SSDEGTCYIE TMNLDGETNL
KIKAAPEETR SLEEADLVGL NAIIDCEGPN SRLYQFTGNL RLRAPLPPTV VAAMAAAQAM
AAAAKAAAAA EAGGGEKEKL EQEGPGWGRA AAKSLLANGM EAHAATLKSM ASTTVAASEP
SRWNFRASQR RASTRVEPPH EYVASLAASA VVLRGCSLRN TTCIYGVVIY AGHDTKIFMN
STEAPSKRSY IERTVDRIIL MFFCVLLIWC LISAVYHAWW TNTHFRQHWY MRPDALDADS
DPDNPAQTGA VNFFVALLLY SYLVPVSLYV SIEMVKVFQA MVLIAQDRDI YHAETDTPAL
ARTSNLNEEL GMVAAVMTDK TGTLTRNVME FFKCSIAGVP YGAGITEIER SNALRKGQVL
DDRERPDAAK FRERFFNFYD DRLMGEAWYS AKDPVTIEMF FRLLAVCHTV IPDGPTDEKS
IKYEAESPDE AALVVAAKAF GFFFFKRTNT TITVRERTPR GTTDVEYEVL NILEFNSTRK
RMSVVVKEKA NEKIIIFCKG ADTVIYERLD PNYGPNEDAK QATTRDMEDF GASGLRTLCL
SYAEVDRDWY DAWAKEWDAG KKSLDDRESK LAEAAEKIER NLRLLGCTAI EDKLQEGVPD
CIRMLALAGI RIWVLTGDKM ETAINIGFAC SLLTEEMHQH TVTASSARVE ELEKAGRRQE
AEALAAELVA KQLDKIDLEL RQATEAATGA AGKAGGAGAG PKQGGAGPGI GGGMGGDAID
AALIIDGKAL SYALSKDLAP LLLRVGLRCK AVVCCRVSPL QKAQVTGLVR STGSITLAIG
DGANDVSMIQ RAHIGVGISG QEGMQAVMSA DFAIAQFRYL VPLLLVHGQY SYKRITRMIN
FFFYKNMLFA ITLFTYSAFT TFSGSYIYND TSMTLFNVAF TSATPLLVGM FDRPLGKRAM
LRYPQLYRQG IANRDFNAAT ILGWMFSALL QSGIILVLCL VGCRGTTASA DHGIPWSMAE
VGVVMFTSIV LTIHLHLTMV EEAWTWVHHL AIWGSVALWY LYLVAFAYFP VSWSLEMWHL
FEGIVAPNAQ FWLYSLIIPA AALLPNFAFR AVSRLLWPSD EDIIREMQKV ERAANSDSSH
RAGGAAGAAA GAASEHHALQ KHKGGGGLLM AAMGSGSNRV APEPPASPLG GGARGGGGAG
VKSAAAIAVA EGGPGNKSFA VTAVIAAGGD GAGAGGAGGG KGKGGRWSAT GQDGVEELDG
EEAADDVTAA PPQPPPGALT GTRSSRDGNP NGFRVVGNKG PGSTMHSASG NGSRAASRAG
PSPFAAALAP PPPGATSNTS GLDELTLVSA DGGGIDGADG GADGRESPLL GSFAPSPTRS
VAGPSVGHIP IAGRSRTAGL PTVGSSTSLV GGAGGVLAGN GHHSQRFAHQ AHLPHAALAS
SISTPVLGED GGRNNSGTGR AAAGAGAGVG PGSSATASPR TQAAVARGQA GTMGSRGGGG
GGEMQPTASM SGGRMVVGQA SGQTGDSASG VREVSTLSRA SSSSVQG
//
