ID A0A3L6SUM3_PANMI Unreviewed; 1239 AA.
AC A0A3L6SUM3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=C2845_PM05G26660 {ECO:0000313|EMBL:RLN28059.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN28059.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(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 -!- 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:RLN28059.1}.
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DR EMBL; PQIB02000003; RLN28059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6SUM3; -.
DR STRING; 4540.A0A3L6SUM3; -.
DR Proteomes; UP000275267; Chromosome 5.
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 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; 2.
DR PANTHER; PTHR24092:SF175; PHOSPHOLIPID-TRANSPORTING ATPASE 9-RELATED; 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:UP000275267};
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 136..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 386..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 954..971
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1033..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1074..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1102..1120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1140..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 86..131
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 919..1169
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 138438 MW; A9D3F66FF360DE3D CRC64;
MAGDQGDDPN PDRRRRRRSR RRAALRLSRL YSFACGRRPS VADDDDASRI GGPGFLRVVN
AGDAALRQQQ QQEQQPSAEQ LLAASSSNSI STTKYNLFTF LPKSLFEQFR RVANVYFLLS
AGIAYSPLAA YSSASAIAPL VIVIVATMLK EAVEDWRRNQ QDTEVNNRST KVFQDGAFRD
ARWKDIRVGD IIKVEKDDFF PADLVLLSSS YEDAICYVET MNLDGETNLK LKQSLEVTSS
SLPDDESFRG FGAVIRCEDP NAHLYSFVGN IEIQDQQQQH PLSPQQLLLR DSKLRNTEFV
YGAVIFTGHD TKVMQNAMKV PSKRSNIERK MDRIIYLLLI SLVLISVVGS IFFGTATRDD
LQDGKMKRWY LRPDDTEIYF DPSKPAIAAV LHFLTAMQLY SYFIPISLYI SIEIVKLLQA
LFINQDIHMY HEESDTPAHA RTSNLNEELG QVDTILTDKT GTLTCNSMEF IKCSIAGTAY
GRGVTEVERA MAKRKGSPLI ADMDSDIQYF QPEGKVAVKG FNFRDERVME GNWVNQPHSN
VIEMFLRLLA VCHTCIPEVD EESGKISYEA ESPDEAAFVV AARELGFTFY QRTQTSVFLH
ELDPVSGKQV DRSYMILNVL EFNSARKRMS VIVKNEEGKI FLFSKGADSV MFERLSGSQT
AYREVTQQHI NEYADAGLRT LVLAYRELEE DEYAYFDRKF TAAKNSISTD RDEKIEEAAD
LLERDLILLG ATAVEDKLQK GVPECVDKLA QAGIKIWVLT GDKMETAINI GYACSLLRQG
MKQIIITLET ADIIALEKGS DKAAITKASK DSVVQQINEG KKLANASAGE TFALIIDGKS
LTYALEDDTK GTFLDLAIGC GSVICCRSSP KQKALVTRLV KTGTGKVTLA IGDGANDVGM
IQEADIGVGI SGAEGMQAVM ASDVSIAQFR FLERLLLVHG HWCYSRISSM ICYFFYKNIT
FGVTLFLYEA YTSFSGQPFY NDWAMASYNV FFTSLPVIAM GVFDQDVSAR FCLKFPMLYQ
EGPQNLLFRW RRIIGWMAYG VGSAVVIFFL STASLQHQAF RRSGEVVDQA TLGATAYTCV
VWAVNLQMAI TVSYFTLVQH ACIWAGVALW YVFLAAYGAI TPTFSTTYHM VFADALAGAP
SYWVVTLLVS AAALVPYFTY AVAKSWFFPD YHNQIQWLRH RERAHPDPES SAHVEFGHAL
RQFSVRSTGV GVSARRDAAV LRRLNGTQVH HADSPQQVS
//
