ALA4_ARATH
ID ALA4_ARATH Reviewed; 1216 AA.
AC Q9LNQ4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable phospholipid-transporting ATPase 4 {ECO:0000303|PubMed:11402198};
DE Short=AtALA4 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 4 {ECO:0000303|PubMed:11402198};
GN Name=ALA4 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g17500 {ECO:0000312|Araport:AT1G17500};
GN ORFNames=F1L3.21 {ECO:0000312|EMBL:AAF79467.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC022492; AAF79467.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29599.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58607.1; -; Genomic_DNA.
DR RefSeq; NP_001319028.1; NM_001332307.1.
DR RefSeq; NP_173193.2; NM_101612.3.
DR AlphaFoldDB; Q9LNQ4; -.
DR SMR; Q9LNQ4; -.
DR BioGRID; 23564; 1.
DR STRING; 3702.AT1G17500.1; -.
DR iPTMnet; Q9LNQ4; -.
DR SwissPalm; Q9LNQ4; -.
DR PaxDb; Q9LNQ4; -.
DR PRIDE; Q9LNQ4; -.
DR ProteomicsDB; 244969; -.
DR EnsemblPlants; AT1G17500.1; AT1G17500.1; AT1G17500.
DR EnsemblPlants; AT1G17500.2; AT1G17500.2; AT1G17500.
DR GeneID; 838324; -.
DR Gramene; AT1G17500.1; AT1G17500.1; AT1G17500.
DR Gramene; AT1G17500.2; AT1G17500.2; AT1G17500.
DR KEGG; ath:AT1G17500; -.
DR Araport; AT1G17500; -.
DR TAIR; locus:2007858; AT1G17500.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q9LNQ4; -.
DR OMA; HNELTSH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9LNQ4; -.
DR BioCyc; ARA:AT1G17500-MON; -.
DR PRO; PR:Q9LNQ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNQ4; baseline and differential.
DR Genevisible; Q9LNQ4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0000287; F:magnesium ion binding; IEA:InterPro.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Isopeptide bond; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1216
FT /note="Probable phospholipid-transporting ATPase 4"
FT /id="PRO_0000046388"
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..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..956
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 957..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 977..1006
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1030..1042
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1043..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1071
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1072..1092
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1093..1109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1110..1134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1135..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1195..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 867
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 871
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SLK6"
SQ SEQUENCE 1216 AA; 138189 MW; FC9B0CD7F96D21E1 CRC64;
MARGRIRSKL RLSHIYTFGC LRPSADEGQD PHPIQGPGFS RTVYCNQPHM HKKKPLKYRS
NYVSTTRYNL ITFFPKCLYE QFHRAANFYF LVAAILSVFP LSPFNKWSMI APLVFVVGLS
MLKEALEDWS RFMQDVKINA SKVYVHKSDG EFRRRKWKKI SVGDIVKVEK DGFFPADLLL
LSSSYEDGIC YVETMNLDGE TNLKVKRSLE VTLSLDDYDS FKDFTGIIRC EDPNPSLYTF
VGNLEYERQI FPLDPSQILL RDSKLRNTPY VYGVVVFTGH DTKVMQNSTK SPSKRSRIEK
TMDYIIYTLL VLLILISCIS SSGFAWETKF HMPKWWYLRP EEPENLTNPS NPVYAGFVHL
ITALLLYGYL IPISLYVSIE VVKVLQASFI NKDLHMYDSE SGVPAHARTS NLNEELGQVD
TILSDKTGTL TCNQMDFLKC SIAGTSYGVR SSEVEVAAAQ QMAVDLDEHG EVSSRTSTPR
AQARDIEVES SITPRIPIKG FGFEDIRLMD GNWLREPHTD DILLFFRILA ICHTAIPELN
EETGKYTYEA ESPDEASFLT AASEFGFVFF KRTQSSVYVH ERLSHSGQTI EREYKVLNLL
DFTSKRKRMS VVVRDEEGQI LLLCKGADSI IFERLAKNGK VYLGPTTKHL NEYGEAGLRT
LALSYRKLDE EEYSAWNAEF HKAKTSIGSD RDELLERISD MIEKDLILVG ATAVEDKLQK
GVPQCIDKLA QAGLKLWVLT GDKMETAINI GYSCSLLRQG MKQICITVVN SEGASQDAKA
VKDNILNQIT KAVQMVKLEK DPHAAFALII DGKTLTYALE DEMKYQFLAL AVDCASVICC
RVSPKQKALV TRLVKEGTGK ITLAIGDGAN DVGMIQEADI GVGISGVEGM QAVMASDFSI
AQFRFLERLL VVHGHWCYKR IAQMICYFFY KNIAFGLTLF YFEAFTGFSG QSVYNDYYLL
LFNVVLTSLP VIALGVFEQD VSSEICLQFP ALYQQGKKNL FFDWYRILGW MGNGVYSSLV
IFFLNIGIIY EQAFRVSGQT ADMDAVGTTM FTCIIWAVNV QIALTVSHFT WIQHVLIWGS
IGLWYLFVAL YGMMPPSLSG NIYRILVEIL APAPIYWIAT FLVTVTTVLP YFAHISFQRF
LHPLDHHIIQ EIKYYKRDVE DRRMWTRERT KAREKTKIGF TARVDAKIRH LRSKLNKKQS
NMSQFSTQDT MSPRSV
