ID A0A0S3RFZ1_PHAAN Unreviewed; 1168 AA.
AC A0A0S3RFZ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-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=Vigan.02G253400 {ECO:0000313|EMBL:BAT79620.1};
GN ORFNames=VIGAN_02253400 {ECO:0000313|EMBL:BAT79620.1};
OS Vigna angularis var. angularis.
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=157739 {ECO:0000313|EMBL:BAT79620.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT79620.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015035; BAT79620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RFZ1; -.
DR Proteomes; UP000291084; Chromosome 2.
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:SF160; 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 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:UP000291084};
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 82..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 356..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1013..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1055..1074
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1081..1100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1120..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..109
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 899..1149
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1168 AA; 132809 MW; 114A6697B6C1C89D CRC64;
MRGGRKRSMI KLKFSKIYSF ACGRTTLRRE HSRIGGHGHS RVVFCNEPDR FEVGVLNYAD
NSVRSTKYTV ATFLPKSLFE QFRRVANFYF LVAGILAFTK LTPYTAVSAI LPLSIIIGAT
MVKEGIEDWR RKKQDIEVNK RRVILHKGDG IFEYTEWKNL RVGNIVKIMK DEFFPADLLL
LSSSYEDAVC YVETMNLDGE TNLKLKQGLD VTSSLQEDFK ICDFRAVIKC EDPNANLYSF
VGSMEFEEQK YPLSAQQLLL RDSKLRNTDY VFGAVIFTGH DTKVIQNSTD PPSKRSKIEK
KMDKIIYFLF CVLFLIAFVG SIIFGIITKG DLKNGLMKRW YLRPDSSTIF FDPERAAAAA
IFHSLTALML YNFFIPISLY FSIEIVKVLQ SIFINQDIHM YYEEADKPAR ARTSNLNEEL
GQVDTILSDK TGTLTCNSME FIKCSVAGVA YGHGVTEVEQ VTGRSNGSPI LHEHINGLKS
KSNEIGDSRD RKEPIKGFNF TDERIMNGNW VNEPFADVIQ KFFRLLAICH TAIPEVDEET
GNVSYEAESP DEAAFVIAAS EVGFKFYKRT QNCLSTYELD PVSGNEVERT YKLLNVLEFS
SSRKRMSVIV KDEEGRILLL SKGADSVMFE RLANSGRTFE EKTMEHVHQY ADAGLRTLIL
SYRELDEEEF KEFDGKLSEV KNSVSEDRET LIEELLDTIE RNLILLGATA VEDKLQNGVP
DCIDKLAQAK IKIWVLTGDK METAINIGFS CRLLRQGMKQ IIIHLDIPEI QALEKVGDKM
AVVKVSRESV HHQLSEGAQL LFASRGTCQQ TFALIIDGKS LTYALEDNMK NMFLELASHC
ASVICCRSSP KQKALVTRLV KSGTGKTTLA IGDGANDVGM LQEADVGIGI SGVEGMQAVM
SSDIAIAQFK YLERLLLVHG HWCYRRMSSM ICYFFFKNIT FGFTLFLYEV YASFSGQPAY
NDWFLSLYSV FFSSLPVIAL GVLDQDVSAR YCLKFPILYQ EGVQNVLFSW RIVLSWMLNG
FINATMIFFF CTKAIEPQAF DEEGRTAGRD MLGVTMYTCV VWVVNLQMAL AIRYFTLIQH
IFIWGSIAFW YLFLLAYGAM PPKFSTNVYQ VFIETLATSP SFWAVTFFVA ISTLIPYFTF
SVIQMWFFPM YHQMVQWIRY ERKTNATE
//
