ID A0A3Q0F417_VIGRR Unreviewed; 1016 AA.
AC A0A3Q0F417;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC106771927 {ECO:0000313|RefSeq:XP_022637157.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022637157.1};
RN [1] {ECO:0000313|RefSeq:XP_022637157.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022637157.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR RefSeq; XP_022637157.1; XM_022781436.1.
DR AlphaFoldDB; A0A3Q0F417; -.
DR Proteomes; UP000087766; Chromosome 1.
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; 1.
DR PANTHER; PTHR24092:SF165; PHOSPHOLIPID-TRANSPORTING ATPASE 8-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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000087766};
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 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 971..988
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 41..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 904..1000
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1016 AA; 115072 MW; 150123AC4A6743C1 CRC64;
MPGGSSKRRI HFSKLYSFSC LKSPFRDGHS QIGQKGYSRV VYCNDPDNPE AVQLSYGGNY
VSTTKYTAFN FIPKSLFEQF RRVANIYFLI VACVSFSPLA PFTALSIVAP LLVVIGATMA
KEAVEDWRRR KQDVEANNRK VQVYGRNYTF TETRWKKLRV GDIIKVYKDE YFPADLLLLS
SSYGDGVCYV ETMNLDGETN LKLKHALEVT VHLHDEKSLQ KFRAMVKCED PNENLYSFIG
TLQHDGKEYP LSLQQILLRD SKLKNTDFIY GIVIFTGHDT KVMQNSTDPP SKRSKIERKM
DKIIYILFST LVLISFIGSV FFGIETKKDI SGGRYRRWYL RPDNATVFYD PRRATLAAVL
HFLTAIMLYG YLIPISLYVS IEIVKVLQSI FINQDQEMYH EESDRPAHAR TSNLNEELGQ
VDTILSDKTG TLTCNSMEFV KCSIGGIAYG RGMTEVEKAL ARRGKGGESD DVDSGSSDFL
GQNNESVDSL HPVKGFNFSD ERLVNGRWVN EPYPDFIQKF FRVLAICHTA IPDEDKESGE
ISYEAESPDE AAFVIAAREL GFEFFARTQT SISLHELNYK SGKKVDSRVY QLLHVLEFSS
SRKRMSVIVR NEENQILLLC KGADSVMFER LSQHGRQFEV ETRDHIKRYA EAGLRTLVVT
YRELDEEEYK LWDKEFSKVK TSVTEDRDAL VDAAADRMER DLMLLGATAV EDRLQKGVPE
CIEKLARAKI KLWVLTGDKM ETAVNIGYAC SLLRKDMKQI VITLDSSDIL YLEKQGDKQA
LAKASLESIK KQIGEGISQI NSAKESSNAN KGSSSGFGLI IDGKSLDYSL NKNLERSFFE
LAINCASVIC CRSSPKQKAR VTRLVKLGTG KTTLSIGDGA NDVGMLQEAD IGVGISGAEG
MQAVMASDFA IAQFRFLERL LLVHGHWCYR RISMMICYFF YKNIAFGFTL FWFEAYASFS
GQAAYNDWYM SFYNVFFTSL PVIALGVFDQ DVSAKLCLKV QGKLIHLRER LKQREL
//
