ID V4KEZ0_EUTSA Unreviewed; 1201 AA.
AC V4KEZ0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=EUTSA_v10018025mg {ECO:0000313|EMBL:ESQ28392.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ28392.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ28392.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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; KI517953; ESQ28392.1; -; Genomic_DNA.
DR RefSeq; XP_006391106.1; XM_006391044.1.
DR AlphaFoldDB; V4KEZ0; -.
DR STRING; 72664.V4KEZ0; -.
DR EnsemblPlants; ESQ28392; ESQ28392; EUTSA_v10018025mg.
DR GeneID; 18009321; -.
DR Gramene; ESQ28392; ESQ28392; EUTSA_v10018025mg.
DR KEGG; eus:EUTSA_v10018025mg; -.
DR eggNOG; KOG0206; Eukaryota.
DR OMA; DMMIYQR; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
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: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:UP000030689};
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 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 932..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1011..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1049..1072
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..110
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 897..1147
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1201 AA; 136336 MW; FB56397A474172C7 CRC64;
MTGTGTTKRR RRRIQLSKLY TLTCAEACFK QDHSQIGGPG FSRVVFINEP DSPEADSRNY
SDNYVRTTKY TLATFLPKSL FEQFRRVANF YFLVTGILSF TPLAPYTAAS AIVPLFFVIG
ATMVKEAVED WRRKKQDIEV NNRKVKVHRG DGNFDSKEWK TLSIGDIVKV EKNEFFPADL
VLLSSSYEDA ICYVETMNLD GETNLKVKQG LEVTTSLREE FDFKGFEAFV KCEDPNANLY
SFVGTMELKG AKYPLSPQQL LLRDSKLRNT DFIYGAVIFT GHDTKVIQNS TDPPSKRSMI
EKKMDKIIYL MFFMVVAMAF IGSVLFGVTT RDDFKDGVMK RWYLRPDSSS IFFDPKRAPV
AAIYHFLTAV MLYSYFIPIS LYVSIEIVKV LQSIFINQDI HMYYEEADKP ARARTSNLNE
ELGQVDTILS DKTGTLTCNS MEFIKCSVAG TAYGRGVTEV EMAMGRRKGS TLVFQSSEND
VEYSKEAVAE EPTVKGFNFR DERIMNGNWV TETHADVIQK FFRLLAVCHT VIPEVDEDTE
KISYEAESPD EAAFVIAARE LGFEFFNRTQ TTISVRELDL VTGKRVERLY KVLNVLEFNS
TRKRMSVIVQ DEDGKLLLLC KGADNVMFER LSKNGREFEE ETRDHVNEYA DAGLRTLILA
YRELDENEYK VFNERISEAK SSVSVDRESL IEEVTEKVEK DLILLGATAV EDKLQNGVPD
CIDKLAQAGI KIWVLTGDKM ETAINIGFAC SLLRQDMKQI IINLETPEIH SLEKTGEKNA
IAKASKENVL LQIINGKSQL NYSGGNSDAF ALIIDGKSLA YALDDDIKHI FLELAVGCAS
VICCRSSPKQ KALVTRLVKS GNGKTTLAIG DGANDVGMLQ EADIGVGISG VEGMQAVMSS
DIAIAQFRYL ERLLLVHGHW CYRRISTMIC YFFYKNITFG FTLFLYEAYT TFSSTPAYND
WFLSLYNVFF SSLPVIALGV FDQDVSARYC LKFPLLYQEG VQNVLFSWRR ILGWMFNGFY
SAVIIFYLCK SSLQSQAFNH DGKTVGREIL GGTMYTCIVW VVNLQMALAI SYFTLIQHIV
IWGSIVVWYI FMAVYGELPA RISTEEYKVF VEALAPSLSY WVITLFVVVS TLMPYFIYSA
IQMSFFPMYH GMIQWLRYEG QCNDPEYCDM VRQRSIRPTT VGFTARLEAK KRSVRRSEPE
S
//
