ALA10_ARATH
ID ALA10_ARATH Reviewed; 1202 AA.
AC Q9LI83;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Phospholipid-transporting ATPase 10 {ECO:0000303|PubMed:11402198};
DE Short=AtALA10 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 10 {ECO:0000303|PubMed:11402198};
GN Name=ALA10 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At3g25610 {ECO:0000312|Araport:AT3G25610};
GN ORFNames=T5M7.5 {ECO:0000312|EMBL:BAB03080.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 SUBCELLULAR LOCATION.
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
CC -!- FUNCTION: Involved in transport of phospholipids.
CC {ECO:0000305|PubMed:11402198}.
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:0000305|PubMed:15308754};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15308754}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; AP001313; BAB03080.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77042.1; -; Genomic_DNA.
DR RefSeq; NP_189189.1; NM_113459.2.
DR AlphaFoldDB; Q9LI83; -.
DR SMR; Q9LI83; -.
DR BioGRID; 7479; 3.
DR STRING; 3702.AT3G25610.1; -.
DR TCDB; 3.A.3.8.24; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9LI83; -.
DR PaxDb; Q9LI83; -.
DR PRIDE; Q9LI83; -.
DR ProteomicsDB; 244810; -.
DR EnsemblPlants; AT3G25610.1; AT3G25610.1; AT3G25610.
DR GeneID; 822148; -.
DR Gramene; AT3G25610.1; AT3G25610.1; AT3G25610.
DR KEGG; ath:AT3G25610; -.
DR Araport; AT3G25610; -.
DR TAIR; locus:2102345; AT3G25610.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9LI83; -.
DR OMA; RDDQREN; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9LI83; -.
DR BioCyc; ARA:AT3G25610-MON; -.
DR PRO; PR:Q9LI83; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LI83; baseline and differential.
DR Genevisible; Q9LI83; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0140333; F:glycerophospholipid flippase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IDA:TAIR.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:1901703; P:protein localization involved in auxin polar transport; IGI:TAIR.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1202
FT /note="Phospholipid-transporting ATPase 10"
FT /id="PRO_0000046394"
FT TOPO_DOM 1..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..954
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1040
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1041..1063
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1064..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1133..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 430
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 865
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 869
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1202 AA; 136279 MW; 5930D14DB7942547 CRC64;
MAGPSRRRRR LHLSKIYSYT CGKSSFQEDH SNIGGPGFSR VVYCNEPGSP AAERRNYAGN
YVRSTKYTVA SFFPKSLFEQ FRRVANFYFL VTGILSLTDL SPYGAVSALL PLALVISATM
VKEGIEDWRR KQQDIEVNNR KVKVHDGNGI FRQEEWRNLR VGDIVRVEKD EFFPADLLLL
SSSYEDSVCY VETMNLDGET NLKVKQGLEA TSSLLNQDSD FKDFRGVVRC EDPNVNLYVF
VGTLALEEER FPLSIQQILL RDSKLRNTEY VYGAVVFTGH DTKVIQNSTD PPSKRSRIER
TMDKIIYLMF GLVFLMSFVG SIIFGVETRE DKVKNGRTER WYLKPDDADI FFDPERAPMA
AIYHFFTATM LYSYFIPISL YVSIEIVKVL QSIFINRDIH MYYEETDKPA QARTSNLNEE
LGMVDTILSD KTGTLTCNSM EFIKCSIAGK AYGRGITEVE RAMAVRSGGS PLVNEDLDVV
VDQSGPKVKG FNFEDERVMN GNWVRQPEAA VLQKFFRLLA VCHTAIPETD EESGNVSYEA
ESPDEAAFVV AAREFGFEFF NRTQNGISFR ELDLVSGEKV ERVYRLLNVL EFNSTRKRMS
VIVRDDDGKL LLLSKGADNV MFERLAKNGR QFEAKTQEHV NQYADAGLRT LVLAYREVDE
NEYIEFNKSF NEAKASVSED REALIDEITD KMERDLILLG ATAVEDKLQN GVPECIDKLA
QAGIKIWVLT GDKMETAINI GFASSLLRQE MKQIIINLET PQIKSLEKSG GKDEIELASR
ESVVMQLQEG KALLAASGAS SEAFALIIDG KSLTYALEDE IKKMFLDLAT SCASVICCRS
SPKQKALVTR LVKSGTGKTT LAIGDGANDV GMLQEADIGV GISGVEGMQA VMSSDIAIAQ
FRYLERLLLV HGHWCYSRIA SMICYFFYKN ITFGVTVFLY EAYTSFSGQP AYNDWFLSLF
NVFFSSLPVI ALGVFDQDVS ARFCYKFPLL YQEGVQNILF SWKRIIGWMF NGFISALAIF
FLCKESLKHQ LFDPDGKTAG REILGGTMYT CVVWVVNLQM ALSISYFTWV QHIVIWGSIA
FWYIFLMIYG AMTPSFSTDA YMVFLEALAP APSYWLTTLF VMIFALIPYF VYKSVQMRFF
PKYHQMIQWI RYEGHSNDPE FVEMVRQRSI RPTTVGYTAR RAASVRRSAR FHDQIYKDLV
GV
