ID A0A5C3LUF7_9AGAR Unreviewed; 1682 AA.
AC A0A5C3LUF7;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BDQ12DRAFT_686994 {ECO:0000313|EMBL:TFK36197.1};
OS Crucibulum laeve.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Nidulariaceae; Crucibulum.
OX NCBI_TaxID=68775 {ECO:0000313|EMBL:TFK36197.1, ECO:0000313|Proteomes:UP000308652};
RN [1] {ECO:0000313|EMBL:TFK36197.1, ECO:0000313|Proteomes:UP000308652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 166.37 {ECO:0000313|EMBL:TFK36197.1,
RC ECO:0000313|Proteomes:UP000308652};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
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; ML213615; TFK36197.1; -; Genomic_DNA.
DR STRING; 68775.A0A5C3LUF7; -.
DR Proteomes; UP000308652; Unassembled WGS sequence.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
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:UP000308652};
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 166..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 517..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 559..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1139..1155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1167..1188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1218..1239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1259..1277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1284..1306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1318..1338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 112..162
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1104..1352
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1682 AA; 187302 MW; F8DB0D4F4D30CA22 CRC64;
MSFLKRNHPP PQDIDTDDEN DENIDPELRL RTVRTAASAI AESIKSEQRA ERRKTMHKKR
SRFFRGRHAE KKPVQPAVAE VVPAKEVPGQ RRNVYVNHPL SAMEVDHDGE PTVRYVRNKV
RTTKYTIFTF IPKNLYEQFR RVANLFFLSL VVLQLFPVFG AASGSIAVLP LAFILTVTAI
KDGVEDYRRG TLDEEVNTSA ATKLDGGWRN VNQPKDPRPW LEKLLGINPP GKVTKGVRKL
RDKEAGEAGK GLRVVLSRTG DDSSVLTHDL GQSSIDLPGR AVGGRRLEDI QSVDSHSYPP
ASLAEVSKTS LSEGSQQLPK GSTEWGQFGS LSQYQQSVHS QSQVGVIDWR KHTGGSARWE
RTLWKKLEVG DIVLLRDNDQ VPADIVVLST SDADGMCYLE TKNLDGETNL KPRKAVKATS
NITSEEDIEK SSFYLDSEPP HQNLYLYHGV LRYRDPSSGD QKQEPVTINE LLLRGCALRN
TAWIIGLVVF TGADTKIMLN GGDTPSKRSK IEKETNFNVL VNFGVLTLMC LIAAIFSGIN
DAKTGTSAEF FEQGSDPTSS FVVNAIITFV SCLIAFQNIV PISLYISIEI VKTIQAYFIS
QDIEMYYRPY DTPCVPKTWN ISDDLGQIEY VFSDKTGTLT QNIMEFQKCS VHGVAYGEGV
TEAQRGAATR EGKADALDPE ALNEKLSSLK RQMLNTMGRA FKNRYLQSDK LTLVSPKLAE
DLTDRSKEQR GHLIAFFRAL ALCHSVLADK PDAQLDPYNL SYKAESPDEA ALVAAARDVG
FPFIGKSKDL FEIEVMGQSE KYTLLKMLEF NSTRKRMSVV MRCPDGRLVL YCKGADSVIY
ARLAKDHDQQ LKEQTSKDME AFANSGLRTL CIAYRWLEEE EYMNWSRTYD AATNAIENRD
EEIDKANELI EHSLQILGAT ALEDKLQEGV PEAIEMLHRA GIKLWILTGD KLQTAIEIGF
SCNLLKNDMD LMILSADTLE QTRAQIEAGL NKIASVLGPP SWDQRKRGFV PGAQASFAVV
IDGDTLRHAL TPELKPLFLN LGTQCETVVC CRVSPAQKAL TVNLVKEGRN AMTLSIGDGA
NDVAMIQEAN IGCGLFGLEG SQAAMSADYA FGQFRFLTKL LLVHGRWSYQ RVADMHSNFF
YKNVIWTFAM FWYLPFNSFD ATYLYQYTFI LLYNLIFTSL PVIILGAFDQ DINAQAALAF
PQLYVRGIRG LEYTRTKFWM YMGDGLYQSA VVFFFPYLVW TLGLSISWNG KGIDSLADFG
TTVSVAAIVA ANTYVGINTH YWTIMTWIVV IGSSLVMLLW IVVYSFFFSS DFIDEVTILF
GTMTFWATVA IAAVIALAPR FIVKYISTVY YPLDKDIVRE MWVKGDLKDQ LGLGHRKEKN
RSKSISPRTL EAAPMFHEQH SRSLSEISMH NPYEPAMTSS PGMGASRQTY LDTPPMSEAG
DVSPRDPAQY VPVQSSLMQE THLSPLPQDN RQQVVSPQPS YYSVSELPPP SPLPSPKYRY
PNGEVTSTPP SRRTSVATTR ASSKTVPQAM PTSPLPEPRT PNTLQLPSVQ PPGLARRMSG
GSPTDPGTFE MRVRSPPLDT PSAQSHGHVF ERSASEVSYA SYMTAPDDYY TAEDDDGEGS
YDRAYGQPHS SSHPQQQHPQ VYDEDDDRAT IVGDNRQDPR RVSAVSAMSA ASAATWQGGR
AL
//
