ID F2DQD2_HORVV Unreviewed; 1151 AA.
AC F2DQD2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAJ97303.1};
RN [1] {ECO:0000313|EMBL:BAJ97303.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Shoot and root {ECO:0000313|EMBL:BAJ97303.1};
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [2] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.3HG0257460.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.3HG0257460.1};
RG EnsemblPlants;
RL Submitted (JAN-2022) 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 EMBL; AK366100; BAJ97303.1; -; mRNA.
DR AlphaFoldDB; F2DQD2; -.
DR EnsemblPlants; HORVU.MOREX.r3.3HG0257460.1; HORVU.MOREX.r3.3HG0257460.1; HORVU.MOREX.r3.3HG0257460.
DR Gramene; HORVU.MOREX.r3.3HG0257460.1; HORVU.MOREX.r3.3HG0257460.1; HORVU.MOREX.r3.3HG0257460.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OMA; FKVAREC; -.
DR Proteomes; UP000011116; Chromosome 3H.
DR ExpressionAtlas; F2DQD2; baseline and differential.
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; 2.
DR PANTHER; PTHR24092:SF207; 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 2: Evidence at transcript level;
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:UP000011116};
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 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 381..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 919..938
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 950..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 996..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1094..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 79..131
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 883..1123
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 128283 MW; 4D9164A05A4B9CC9 CRC64;
MTSERPLIDA ASPHLPAAAS QLPPSQPEPP VRADHLGLSV DVPDPFRSSR RDHPDPSASE
RELHEGGEYR AVAVGEPSPE FDGNSVRTAK YSALTFLPRN LFEQFRRLSY VYFLAITVLN
QLPQVAVFGR GASVLPLAFV LFVTAVKDAY EDIRRHRSDR RENNRLAVVL APQTAGEFLP
KKWKHIRVGD VVRFASNETL PADMVLLATS DPTGLAHVQT VNLDGETNLK TRYAKQETQL
RFSQDGHVAG ILHCERPNRN IYGFQANLEI DGKRVSLGPS NIVLRGCELK NTTWAIGVVV
YAGKETKVML NNSGPPSKRS RLETQLNRET VILSIMLIGM CITASVLAGI WLLNHQRELE
FTQFFREKDY TTGKNYNYYG IGMQIFVTFL MAVIVYQVII PISLYISMEL VRLGQAYFMG
ADNDLYDGSS RSRFQCRALN INEDLGQIKY VFSDKTGTLT ENKMEFVCAS IHGVDYSSGK
HACGYSVVVR TDPQLLKLLS NHSSNGEAKF VLEFFLALAA CNTIVPLVLD TRDPRQKLID
YQGESPDEQA LAYAAASYGI VLVERTSGYV VIDVLGDRQR YDVLGLHEFD SDRKRMSVIV
GCPDKTVKLY VKGADSSMFG IINSLELDNV RATEAHLHKY SSLGLRTLVV GMRELSQPEF
EEWQLAYEKA STAVLGRGNL LRSIAANVEC NIHILGASGI EDKLQDGVPE AIESLRQAGM
KVWILTGDKQ ETAISIGYSC KLLTNDMTQI VINNNSKESC KKSLEEALAR TKEHRVASSI
GSPNPVFATE SSGTVLALIV DGNSLVYILE TELQEELFKV ATECSAVLCC RVAPLQKAGI
VALIKNRTDD MTLAIGDGAN DVSMIQMADV GVGISGQEGG QAVMASDFSM GQFRFLVPLL
LVHGHWNYQR MGYMILYNFY KNATFVLVLF WYVLYTSFTL TTAITEWSSL LYTVLYTSLP
TIIVGILDKD LSKSTLLAYP KLYGSGQRNE KYNLNLFVLN MLEALWQSLI VFYIPYFAYR
QSTIGMSSLG DLWALASVIV VNMQLAMDII QWNWIIHAFI WGTIAATVIC LFVIDSIWVL
PGYGVIYHIM GQGLFWLLLL IIVVTAMVPH FAIKAFMEHF VPTDIQIGQE IEKFKALNQV
NRSEIPMRTF S
//
