ID A0A1S3U0P8_VIGRR Unreviewed; 1214 AA.
AC A0A1S3U0P8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC106760704 {ECO:0000313|RefSeq:XP_014499595.1};
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_014499595.1};
RN [1] {ECO:0000313|RefSeq:XP_014499595.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014499595.1};
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}.
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DR RefSeq; XP_014499595.1; XM_014644109.2.
DR AlphaFoldDB; A0A1S3U0P8; -.
DR STRING; 3916.A0A1S3U0P8; -.
DR GeneID; 106760704; -.
DR KEGG; vra:106760704; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000087766; 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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF208; 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 PRINTS; PR00121; NAKATPASE.
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 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 371..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 429..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1008..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1054..1078
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1084..1103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1110..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1141..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 115..182
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 941..1181
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 135683 MW; 2C63E2745E8D40C9 CRC64;
MGSKRPHVIM TPSTAAPDNY QLDPFSVNIP EQPTSNSSFG NVFNPFENSL VSSSSRRSSM
SNRSSGSKSN NSIHEVSLSG SASKSIPVRY GSKGADSEGL SVSQRELRDE DARLVYINDP
LKTNETFLFA GNSIRTSKYS LLSFIPRNLF EQFHRIAYVY FLIIAILNQL PQLAVFGRAV
SILPLSFVLF VTAVKDAYED WRRHRSDKVE NNRLASVLVD GNFLEKSWRD IRVGEVIKIK
ANEPIPCDIV LLSTSDPTGV AYVQTINLDG ESNLKTRYAK QETHGKEGFG GVIKCEKPNR
NIYGFLANME VDGKKLSLGS SNIVLRGCEL KNTSWAIGVA AYCGSETKAM LNSSGAPSKR
SRLETRMNFE IIWLSVFLVA LCTITSVCAA VWLKRHKDEL NLLPYYRKLD FSEEGEVESY
EYYGWGLEVL FTFLMSVIVF QVMIPISLYI SMELVRVGQA FFMIRDNRMY DEETKSRFQC
RALNINEDLG QIKYVFSDKT GTLTQNKMEF QCASIWGVDY SSTENGMEGD QVEHSVEVDG
KVFRPKMKVK VNPELLQLAR SGFLNLEGKR IHDFFLALAT CNTIVPIVVD SPDPDVKLID
YQGESPDEQA LAYAAAAYGF MLIERTSGHI VIDIHGKRQK FNVLGLHEFD SDRKRMSVIL
GYPDNSVKVF VKGADTSMLN VIDKSFSMHL VRATEAHLHS YSSIGLRTLV IGMRDLNTSE
FEQWHASFEA ASTAVFGRAA MLRKVSSIVE NSLSILGASA IEDKLQQGVP ESIESLRIAG
IKVWVLTGDK QETAISIGYS SKLLTSKMNQ IIINSNNRAA CRKSLQDALV MSKKLMSTSS
VANNSGGGSE ANPIALIIDG TSLVHILDSE LEEELFQLAS RCSVVLCCRV APLQKAGIVA
LVKNRTSDMT LAIGDGANDV SMIQMADVGV GISGQEGRQA VMASDFAMGQ FRFLVPLLLI
HGHWNYQRLG YMILYNFYRN AVLVLVLFWY VLYTAFTLTT AINEWSTTLY SIIYSSLPTI
VVAILDKDLG KRTLLKYPQL YGAGQRHEAY NKKLFALTML DTLWQSMVIF WAPLFAYWSS
TVDVSSIGDL WTFGVVILVN LHLAMDVVRW YWVTHVAIWG SIVATFISVM IIEAFPNLPG
YWAFFNAAGT GLFWLLLLGI IIAALLPRLV VKYVYEYYFP NDIQICREAE KIEYERVVES
AAIEMLPISN IPPR
//
