ID A0A4U6VBJ9_SETVI Unreviewed; 1022 AA.
AC A0A4U6VBJ9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=SEVIR_4G165700v2 {ECO:0000313|EMBL:TKW21337.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW21337.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKW21337.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) 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 -!- 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; CM016555; TKW21337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6VBJ9; -.
DR EnsemblPlants; TKW21337; TKW21337; SEVIR_4G165700v2.
DR Gramene; TKW21337; TKW21337; SEVIR_4G165700v2.
DR Proteomes; UP000298652; Chromosome 4.
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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
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:SF175; 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000298652};
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 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 747..764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 826..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 894..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 933..956
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 712..962
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1022 AA; 116454 MW; 2ECAB960C4C71B21 CRC64;
MEEHQSWRCN KETMNLDGET NLKIKQALEV TSDLQEDIKF REVRQTIKCE DPNANLYSFV
GSMEWKGQRH PLSPQQLLLR DSKLRNTDYI YGAVIFTGHD TKVMQNATDP PSKRSKIEKK
MDKIIYLLMS SLLMIALLGS VFFGIWTKED LRDGEIKRWY LRPDATTIFY DPKRAALASF
FHLLTALMLY SYFIPISLYI SIEMVKLLQA LFINQDIEMY HEESDKPTHA RTSNLNEELG
MVDTILSDKT GTLTCNMMEF IKCSIAGTAY GQGVTEVERA MAMRKGARLD DDIENGDHKD
KKVDDSPHVK GFNFKDPRIM DGNWTNEPNR DMIRDFFRLL AICHTCIAEI DETGKVSYEA
ESPDEAAFVI AARELGFEFY KRSPTTIIVR ERDPSQNVVE KRKYDLLNIL EFSSSRKRMS
VIVKEPEGRI LLFSKGADSV MFKRLAPDGR KFEEDTRRHI NEYSDSGLRT LVLAYRVLDE
KEYKEFNEKL NDAKTSVSAD RDEKIEQAAD SIEQDLILLG ATAVEDKLQK GVPECIDKLA
QAGIKIWVLT GDKMETAINI GFACSLLRQG MTQIIVTLEQ PDIIALEKNG DKQAIAKASK
QRVMDQIEDG IEKIPPSTQT STASFALIID GKSLTYALED DVKFKFLDLA IKCASVICCR
SSPKQKALVT RLVKEVTHKV TLAIGDGAND VGMLQEADIG VGISGAEGMQ AVMASDVAVA
QFRFLERLLL VHGHWCYRRI SVMICYFFYK NVTFGVTIFL YEAFASFSGK PAYNDWFLSL
YNVFFTSLPV IALGVFDQDV SARLCIQYPQ LYQEGVQNIL FSWRRILGWM LNGVMNAVLI
FFFCITAFED QAFRQDGQVA GLDALGVVMY TCVVWVVNCQ MALSVNYFTI IQHIFIWGSI
AVWYLFLLVY GAINPRFSTT AYMVFIEQLA PALSFWLVTL FVVMATLVPY FSYAAIQIRF
FPMFHNKIQW KRYLGKAEDP EVARQLSSRH RTSSQQRMVG ISARRDGKAM QITRETELEV
QE
//