ID K7MGG6_SOYBN Unreviewed; 1173 AA.
AC K7MGG6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=100792960 {ECO:0000313|EnsemblPlants:KRH07629};
GN ORFNames=GLYMA_16G099700 {ECO:0000313|EMBL:KRH07629.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH07629};
RN [1] {ECO:0000313|EMBL:KRH07629.1, ECO:0000313|EnsemblPlants:KRH07629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH07629};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH07629.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH07629}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH07629};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH07629.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH07629.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000849; KRH07629.1; -; Genomic_DNA.
DR RefSeq; XP_003548741.1; XM_003548693.3.
DR RefSeq; XP_006599229.1; XM_006599166.2.
DR AlphaFoldDB; K7MGG6; -.
DR SMR; K7MGG6; -.
DR STRING; 3847.K7MGG6; -.
DR PaxDb; 3847-GLYMA16G19180-3; -.
DR EnsemblPlants; KRH07629; KRH07629; GLYMA_16G099700.
DR GeneID; 100792960; -.
DR Gramene; KRH07629; KRH07629; GLYMA_16G099700.
DR KEGG; gmx:100792960; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; K7MGG6; -.
DR OMA; DGIEDWH; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000008827; Chromosome 16.
DR ExpressionAtlas; K7MGG6; baseline.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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: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:UP000008827};
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 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 931..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1010..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1052..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1117..1140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 43..108
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 896..1146
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1173 AA; 132832 MW; D8C89B9D35DE4619 CRC64;
MSGGRRRKLR LSKIYSFACC KASFEGDHHS QIGGKGYSRV VFCNEPDSFV EDGVKNFADN
SVRSTKYTLA TFFPKSLFEQ FRRAANFYFL VTGTLAFTKL APYTAVSAIL PLIIVIGATM
VKEGIEDLCR KKQDIEVNNR RVKVHKADGI FEYTAWKNVR VGNIVKVEKD EFFPADLLLL
SSSYDDAVCY VETMNLDGET NLKLKQGLEV TSSLQEDLHF LNFKATVKCE DPNANLYSFV
GSMDFEEKNN ALSPQQLLLR DSKLRNTDYI FGAVIFTGHD TKVIQNSTDP PSKRSRIEKK
MDRVIYFLFC ILFLMAFVGS IFFGIATKDD FQNGLMKRWY LTPDDSTVFF DPKRPAAAAL
FHCLTALMLY GFFIPISLYV SIEIVKVLQS IFINQDIHMY YREADKPARA RTSNLNEELG
QVDTILSDKT GTLTCNSMEF IKCSIAGVAY GRGATEVEKA MDRRKGSPSI HEHDIESEAD
NIRGSLDKRA LIKGFNFADE RITNGNWVNE PHADVIQKFF RLLVVCHTAI PEVDEETGNV
SYEAESPDEA AFVIAARELG FEFYKRGQTS LLTYELDPVS CKKVERKYKL LNCLEFNSSR
KRMSVIVEDE EGKILLLCKG ADSIMFERLA KNGREFEEKT MEHVHEYADA GLRTLILAYR
ELDAEEYKEF DNKFSMAKNL VSADQDILIE EVSEKIEKNL ILLGATAVED KLQDGVPECI
DKLARAGIKI WVLTGDKMET AINIGFACSL LRQGMKQIII HLDSPEIQAL EKDGDKMAIA
KASRQSVLLQ ISDGAAQLTA YRGSSHQAFA LIIDGKSLAY ALEDNMKNMF LELAIRCASV
ICCRSSPKQK AMVTRLVKSG ARKTTLAIGD GANDVGMLQE ADIGVGISGV EGMQAVMSSD
IAIAQFRYLE RLLLVHGHWC YRRISSMICY FFYKNITFGF TLFLYEVYAS FSGQAAYNDW
FLSLYNVFFS SLPVIALGVF DQDVSARYCL KFPLLYQEGV QNVLFSWRRI LSWMLNGFIS
ALIIFFFCTK AMELQAFDVE GRTAGKDILG AAMYTCVVWV VNLQMALAVS YFTMIQHFFI
WGSILLWYLF LVVYGAMPPH FSTNAYKVFI EALAPSPSYW IVTLFVVIST LIPYFSYAAI
RMRFFPMYHE TVQWIRYEGK IKDPEFLSVQ QHA
//
