ID A0A369JJ38_HYPMA Unreviewed; 1358 AA.
AC A0A369JJ38;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Hypma_010733 {ECO:0000313|EMBL:RDB22221.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB22221.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB22221.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB22221.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RDB22221.1}.
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DR EMBL; LUEZ02000052; RDB22221.1; -; Genomic_DNA.
DR STRING; 39966.A0A369JJ38; -.
DR InParanoid; A0A369JJ38; -.
DR Proteomes; UP000076154; 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 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; 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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF153; 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 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.
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:UP000076154};
KW Translocase {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 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1001..1020
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1032..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1083..1105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1149..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1182..1204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 54..111
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 969..1219
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 151669 MW; 9EEFC37DF6769113 CRC64;
MASTKAGAFA TWYSRIAAFK VEDIFSQKRL PGPPRTVFVN EDIPEHYFDH KGRHKADYVY
TSNQVITSKY TVITFLPRNL LEQFRRIANM FFLAIATLQF FPKFSTIAPG VVILPLIIIL
AVTAFKDGYE DIKRHQSDKR VNQSSVRVLA GGDWNNANGM QAKTKTFVRG LVRPLRRTRK
PDSSQAAQAY SDEDIEFDGD GPDVADEKRG RLSPHWEKTL WEDLHVGDIV KIIDNEPFPA
DILICATSEE TKTSLPALSH LRDAAKCADR KNSFRLNCDR PDTDMYRMKA NVTVDGDVSP
IDMSMMLLRG TVLRNTRWVI GIVLYTGLDT KIVMNSGGTP SKRSKVEAQM NPQVFFNLTI
MALMAVVCAI ADSLLEVKYF PLQAPWLFGD DLSDDNPRIN GLITWAYSLL TFQTIVPISL
YISIEFVRTC QAAFIYFDAD ISYEKTGQAT ISRSWNLSDD LGQIEYIFSD KTDTLTQNSM
VFRQCSIGGV AYRGDVESLD APEELAPEID SVKPFSITAN AEKDDRSVEV NVWAAAAASS
KSAIIMESSP KLPYKMPTKP NDAIVRFRDS SLYHDIEAAV DVDPDSEGAT HARLLNGFFT
VLALCHTVLT SVDPLTGQIE YKAQSPDEAA LVQAAADVSF VFSGRDRETL TLRTPSSAPD
VEKYELLNIL EFTSARKRMS VVLRKLGGED GQLFLLTKGA DNVIFQRLRA SERELMDETE
EHLSEFANGV SMDDREARIE AVSNELEQDL RLLGATAIED RLQDGVPETI ADLKRTGIRI
WVATGDKLET AIAIGRSTNL IASDSNIIII RGGIETGRPV HQQMTHAMSK YFLDSGIIGE
DLPRPSTSSR DADRHHIPLQ RITTGTSSVV GAGNGDRPGG FVLVIDGAAL LHAFEDEQNK
ALLLRLATLC EGVICCRVSP LQKALVVRLV KDGLGAMTLA IGDGANDVSM IQAADVGVGI
SGEEGLQAVN SSDYAIAQFR FLKKLLLVHG HWSYARNGTM ILNFFYKNVV PVGILWWFQI
YEGWSGYFVF DYIYILFWNS IWTIAPVIGI GLFDRFLDSH VLMDVPELYH YGRRGTWFGL
KSFFIYMFDG LFQSVIIFFL IVYAYKSPTA RKDGYDVHLT EFSTTMAIAG VMVADIFTGL
SATAWTAWLF FAVFIGIFIV WMFTIIYSLI SPGYAVTSLY GNYYLLFTSA KFWLSIPLTF
CLALTPRLIT KCYQVGFAPD DLNTIRWVNK FEPDLDLKHD AHVTHLSALK RPPSAASRRT
SRSYVNDSTA TVNLRRQSVD VRAASRTDMA TGLVSIDRGF DFAMEEHGVA MRRMQSNLSE
RRSGRNLAPM SPLHEKGKST LSQMFSLRRK RKGPRKSE
//
