ID ALA9_ARATH Reviewed; 1200 AA.
AC Q9SX33;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Putative phospholipid-transporting ATPase 9 {ECO:0000303|PubMed:11402198};
DE Short=AtALA9 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 9 {ECO:0000303|PubMed:11402198};
GN Name=ALA9 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g68710 {ECO:0000312|Araport:AT1G68710};
GN ORFNames=F24J5.6 {ECO:0000312|EMBL:AAD49973.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
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: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AC008075; AAD49973.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34830.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58269.1; -; Genomic_DNA.
DR PIR; F96711; F96711.
DR RefSeq; NP_001320717.1; NM_001334377.1.
DR RefSeq; NP_177038.1; NM_105543.6.
DR AlphaFoldDB; Q9SX33; -.
DR SMR; Q9SX33; -.
DR STRING; 3702.Q9SX33; -.
DR iPTMnet; Q9SX33; -.
DR PaxDb; 3702-AT1G68710-1; -.
DR ProteomicsDB; 244982; -.
DR EnsemblPlants; AT1G68710.1; AT1G68710.1; AT1G68710.
DR EnsemblPlants; AT1G68710.2; AT1G68710.2; AT1G68710.
DR GeneID; 843201; -.
DR Gramene; AT1G68710.1; AT1G68710.1; AT1G68710.
DR Gramene; AT1G68710.2; AT1G68710.2; AT1G68710.
DR KEGG; ath:AT1G68710; -.
DR Araport; AT1G68710; -.
DR TAIR; AT1G68710; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q9SX33; -.
DR OMA; DMMIYQR; -.
DR PhylomeDB; Q9SX33; -.
DR PRO; PR:Q9SX33; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX33; baseline and differential.
DR Genevisible; Q9SX33; AT.
DR GO; GO:0016020; C: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:1901703; P:protein localization involved in auxin polar transport; IGI:TAIR.
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; 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; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1200
FT /note="Putative phospholipid-transporting ATPase 9"
FT /id="PRO_0000046393"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..945
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 946..959
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 960..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1010..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1045
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1046..1068
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1069..1074
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1113..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 430
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 870
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 874
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1200 AA; 136045 MW; E8CAB216E2D2B261 CRC64;
MVGGGTKRRR RRLQLSKLYT LTCAQACFKQ DHSQIGGPGF SRVVYCNEPD SPEADSRNYS
DNYVRTTKYT LATFLPKSLF EQFRRVANFY FLVTGVLAFT PLAPYTASSA IVPLLFVIGA
TMVKEGVEDW RRQKQDNEVN NRKVKVHRGD GSFDAKEWKT LSIGDIVKVE KNEFFPADLV
LLSSSYEDAI CYVETMNLDG ETNLKVKQGL EVTSSLRDEF NFKGFEAFVK CEDPNANLYS
FVGTMELKGA KYPLSPQQLL LRDSKLRNTD FIFGAVIFTG HDTKVIQNST DPPSKRSMIE
KKMDKIIYLM FFMVITMAFI GSVIFGVTTR DDLKDGVMKR WYLRPDSSSI FFDPKRAPVA
AIYHFLTAVM LYSYFIPISL YVSIEIVKVL QSIFINQDIH MYYEEADKPA RARTSNLNEE
LGQVDTILSD KTGTLTCNSM EFIKCSVAGT AYGRGVTEVE MAMGRRKGGP LVFQSDENDI
DMEYSKEAIT EESTVKGFNF RDERIMNGNW VTETHADVIQ KFFRLLAVCH TVIPEVDEDT
EKISYEAESP DEAAFVIAAR ELGFEFFNRT QTTISVRELD LVSGKRVERL YKVLNVLEFN
STRKRMSVIV QEEDGKLLLL CKGADNVMFE RLSKNGREFE EETRDHVNEY ADAGLRTLIL
AYRELDEKEY KVFNERISEA KSSVSADRES LIEEVTEKIE KDLILLGATA VEDKLQNGVP
DCIDKLAQAG IKIWVLTGDK METAINIGFA CSLLRQDMKQ IIINLETPEI QSLEKTGEKD
VIAKASKENV LSQIINGKTQ LKYSGGNAFA LIIDGKSLAY ALDDDIKHIF LELAVSCASV
ICCRSSPKQK ALVTRLVKSG NGKTTLAIGD GANDVGMLQE ADIGVGISGV EGMQAVMSSD
IAIAQFRYLE RLLLVHGHWC YRRISTMICY FFYKNITFGF TLFLYETYTT FSSTPAYNDW
FLSLYNVFFS SLPVIALGVF DQDVSARYCL KFPLLYQEGV QNVLFSWRRI LGWMFNGFYS
AVIIFFLCKS SLQSQAFNHD GKTPGREILG GTMYTCIVWV VNLQMALAIS YFTLIQHIVI
WSSIVVWYFF ITVYGELPSR ISTGAYKVFV EALAPSLSYW LITLFVVVAT LMPYFIYSAL
QMSFFPMYHG MIQWLRYEGQ CNDPEYCDIV RQRSIRPTTV GFTARLEAKK RSVRISEPAS
//
