ID V7B3C3_PHAVU Unreviewed; 1288 AA.
AC V7B3C3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PHAVU_008G081700g {ECO:0000313|EMBL:ESW12065.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW12065.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|EMBL:ESW12065.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002295; ESW12065.1; -; Genomic_DNA.
DR EMBL; CM002295; ESW12066.1; -; Genomic_DNA.
DR RefSeq; XP_007140071.1; XM_007140009.1.
DR RefSeq; XP_007140072.1; XM_007140010.1.
DR STRING; 3885.V7B3C3; -.
DR EnsemblPlants; ESW12065; ESW12065; PHAVU_008G081700g.
DR EnsemblPlants; ESW12066; ESW12066; PHAVU_008G081700g.
DR GeneID; 18622214; -.
DR Gramene; ESW12065; ESW12065; PHAVU_008G081700g.
DR Gramene; ESW12066; ESW12066; PHAVU_008G081700g.
DR KEGG; pvu:PHAVU_008G081700g; -.
DR eggNOG; KOG0206; Eukaryota.
DR OMA; QALRCGR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000000226; Chromosome 8.
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; 3.
DR PANTHER; PTHR24092:SF148; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000000226};
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 420..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 478..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1062..1083
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1135..1153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1165..1184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1191..1213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1233..1252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 158..223
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1022..1262
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 145464 MW; FAF64CABEAD0CE24 CRC64;
MSSDESLLLE SDPRPVIHHR RGKSGSRTYL CGHGSFSSSV FEAALADISD LDVKERNKEA
VLASDCSFHP ASFSNSNCSD TCAVESKFPW ECPTRERRRS ASWGAMELHD ADSRSVPFEI
SGGASHVQDR LNSKSQRIRH RSVQFDDPAF QEDGARLIYI NDPRKTNDKY EFTGNEIRTS
RYTFVTFLPK NLFIQFHRVA YLYFLAIAAL NQLPPLAVFG RTVSLFPLLF VLCVTAIKDG
YEDWRRHRSD RNENNRESLV LQSGDFRSKK WKKIQAGEVV KIFADETIPA DMVLLGTSDQ
SGLAYIQTMN LDGESNLKTR YARQETASVV ASESCDVFGV IRCEQPNRNI YEFTANMEFN
GLKFSLSQSN IVLRGCQLKN TDWIIGVVVY AGQETKAMLN SAASPSKRSR LECYMNRETL
WLSVFLFIMC LVVALGMCLW LVRHKNQLDT LPYYRKRYFT NGPDNGKRYK YYGIPMEAFF
SFLSSVIVFQ IMIPISLYIT MELVRLGQSY FMIEDRDMYD ASSGSRFQCR SLNINEDLGQ
IRYIFSDKTG TLTENKMEFR RASIHGKNYG SSLPMVDNTA AADVTPKRRW KLKSEIAVDS
ELMIMLQGNA DREERVSGHE FFLTLAACNT VIPIHGDGGF SSCGTTGLNE DIRRIDYQGE
SPDEQALVSA ASAYGYTLFE RTSGHIVIDV NGEKLRLDVL GLHEFDSVRK RMSVVIRFPD
NAVKVLVKGA DSSMFSILEN GRESNNRIQH TTQSHLNEYS SEGLRTLVIG SRDLSDAELE
EWQSRYEEAS TSLTDRATKL RQTAALIESN LKLLGATGIE DKLQEGVPEA IEALRQAGIK
VWVLTGDKQE TAISIGLSCK LLSGDMQQII INGTSEVECR NLLADAKAKY GVKSSSGGRR
SLKHKTNAGH GDLLDIPNGF PKWTPGKEEG TIAPLALIID GNSLVYILEK ELESELFDLA
ISCRVVLCCR VAPLQKAGIV DLIKSRTDDM TLAIGDGAND VSMIQMADVG VGICGQEGRQ
AVMASDFAMG QFQFLKKLLL VHGHWNYQRV GYLVLYNFYR NAVFVLMLFW YILCTAFSTT
SALTDWSSVF YSVIYTSVPT IIVGIQDKDL SHRTLLQYPK LYGSGHRQEA YNMQLFWITM
IDTVWQSLVL FYIPLFTYKD SSIDIWSMGS LWTIAVVILV NVHLGMDINR WVLITHFAIW
GSIIITYGCM VILDSIPVFP NYWTIYNLAR SPTYWVTILL IIIVSLLPRF ICKVVYQIFW
PSDIQIAREA ELMRKRQANL RPRQQVSS
//
