ID ALA7_ARATH Reviewed; 1243 AA.
AC Q9LVK9; F4JEL2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Probable phospholipid-transporting ATPase 7 {ECO:0000303|PubMed:11402198};
DE Short=AtALA7 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 7 {ECO:0000303|PubMed:11402198};
GN Name=ALA7 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At3g13900 {ECO:0000312|Araport:AT3G13900};
GN ORFNames=MDC16.2 {ECO:0000312|EMBL:BAB02320.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11402198; DOI=10.1104/pp.126.2.696;
RA Axelsen K.B., Palmgren M.G.;
RT "Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
RL Plant Physiol. 126:696-706(2001).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=25954280; DOI=10.3389/fpls.2015.00197;
RA McDowell S.C., Lopez-Marques R.L., Cohen T., Brown E., Rosenberg A.,
RA Palmgren M.G., Harper J.F.;
RT "Loss of the Arabidopsis thaliana P4-ATPases ALA6 and ALA7 impairs pollen
RT fitness and alters the pollen tube plasma membrane.";
RL Front. Plant Sci. 6:197-197(2015).
CC -!- FUNCTION: Involved in transport of phospholipids and in regulation of
CC pollen plasma membrane lipid asymmetry. {ECO:0000305|PubMed:25954280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:11402198};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9SLK6};
CC Multi-pass membrane protein {ECO:0000255}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9SLK6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Ala6 and ala7 double mutants are hypersensitive
CC to temperature stress and are impaired in pollen fitness with an
CC altered lipid composition and short and slow pollen tubes.
CC {ECO:0000269|PubMed:25954280}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02320.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019229; BAB02320.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75436.1; -; Genomic_DNA.
DR RefSeq; NP_188006.4; NM_112244.5.
DR AlphaFoldDB; Q9LVK9; -.
DR SMR; Q9LVK9; -.
DR STRING; 3702.Q9LVK9; -.
DR PaxDb; 3702-AT3G13900-1; -.
DR ProteomicsDB; 245016; -.
DR EnsemblPlants; AT3G13900.1; AT3G13900.1; AT3G13900.
DR GeneID; 820603; -.
DR Gramene; AT3G13900.1; AT3G13900.1; AT3G13900.
DR KEGG; ath:AT3G13900; -.
DR Araport; AT3G13900; -.
DR TAIR; AT3G13900; ALA7.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q9LVK9; -.
DR OMA; PYGAFYS; -.
DR OrthoDB; 275833at2759; -.
DR BioCyc; ARA:AT3G13900-MONOMER; -.
DR PRO; PR:Q9LVK9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVK9; baseline and differential.
DR Genevisible; Q9LVK9; AT.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR GO; GO:1905038; P:regulation of membrane lipid metabolic process; IGI:TAIR.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF173; PHOSPHOLIPID-TRANSPORTING ATPASE 7-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; 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; Cell membrane; Isopeptide bond; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1243
FT /note="Probable phospholipid-transporting ATPase 7"
FT /id="PRO_0000046391"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962..975
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..995
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 996..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1049..1061
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1062..1084
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1085..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1129..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1154..1243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 425
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 886
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 890
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SLK6"
FT CONFLICT 614
FT /note="V -> F (in Ref. 1; BAB02320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1243 AA; 140301 MW; C6BCC3D8BD909E08 CRC64;
MGRRRIRSRI RKSHFYTFKC LRPKTLEDQG PHIINGPGYT RIVHCNQPHL HLAKVLRYTS
NYVSTTRYNL ITFLPKCLYE QFHRVANFYF LVAAILSVFP LSPFNKWSMI APLIFVVGLS
MGKEALEDWR RFMQDVKVNS RKATVHRGDG DFGRRKWKKL RVGDVVKVEK DQFFPADLLL
LSSSYEDGIC YVETMNLDGE TNLKVKRCLD VTLPLERDDT FQSFSGTIKC EDPNPNLYTF
VGNLEYDGQV YPLDPSQILL RDSKLRNTSY VYGVVVFTGH DTKVMQNSTK SPSKRSRIEK
RMDYIIYTLF ALLVLVSFIS SLGFAVMTKM HMGDWWYLRP DKPERLTNPR NPFHAWVVHL
ITAVLLYGYL IPISLYVSIE LVKVLQATFI NQDLQMYDSE SGTPAQARTS NLNEELGQVD
TILSDKTGTL TCNQMDFLKC SIAGTSYGVR ASEVELAAAK QMAIDLDEEQ GEEVTHLPRT
RGRMHGYAKM PSKTSSDIEL ETVITATDEG DQTQSTGIKG FSFEDQRLMG GNWLNEPNSD
DILMFLRILA VCHTAIPEVD EDTGKCTYEA ESPDEVAFLV AAGEFGFEFT KRTQSSVFIS
ERHSGQPVER EYKVLNVLDF TSKRKRMSVI VRDEKGQILL LCKGADSIIF ERLSKNGKNY
LEATSKHLNG YGEAGLRTLA LSYRKLDETE YSIWNSEFHK AKTSVGADRD EMLEKVSDMM
EKELILVGAT AVEDKLQKGV PQCIDKLAQA GLKIWVLTGD KMETAINIGY ACSLLRQGMK
QIYIALRNEE GSSQDPEAAA RENILMQIIN ASQMIKLEKD PHAAFALIID GKTLTYALED
DIKYQFLALA VDCASVICCR VSPKQKALVT RLAKEGTGKT TLAIGDGAND VGMIQEADIG
VGISGVEGMQ AVMASDFSIA QFRFLERLLV VHGHWCYKRI AQMICYFFYK NITFGLTLFY
FEAFTGFSGQ AIYNDSYLLL FNVILTSLPV IALGVFEQDV SSEVCLQFPA LYQQGPKNLF
FDWYRIIGWM ANGVYASVVI FSLNIGIFHV QSFCSGGQTA DMDAMGTAMF TCIIWAVNVQ
IALTMSHFTW IQHVLIWGSI VTWYIFLALF GMLPPKVSGN IFHMLSETLA PAPIFWLTSL
LVIAATTLPY LAYISFQRSL NPLDHHIIQE IKHFRIDVQD ECMWTRERSK AREKTKIGVT
ARVDAKIRQL RGRLQRKHSI LSVMSGLSGV SASTDTTSTT QHS
//
