ALA5_ARATH
ID ALA5_ARATH Reviewed; 1228 AA.
AC Q9SGG3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable phospholipid-transporting ATPase 5 {ECO:0000303|PubMed:11402198};
DE Short=AtALA5 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 5 {ECO:0000303|PubMed:11402198};
GN Name=ALA5 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g72700 {ECO:0000312|Araport:AT1G72700};
GN ORFNames=F28P22.11 {ECO:0000312|EMBL:AAG51844.1};
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; AC010926; AAG51844.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35362.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60518.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60519.1; -; Genomic_DNA.
DR PIR; G96751; G96751.
DR RefSeq; NP_001322799.1; NM_001334547.1.
DR RefSeq; NP_001322800.1; NM_001334546.1.
DR RefSeq; NP_177414.1; NM_105929.5.
DR AlphaFoldDB; Q9SGG3; -.
DR SMR; Q9SGG3; -.
DR BioGRID; 28821; 1.
DR STRING; 3702.AT1G72700.1; -.
DR iPTMnet; Q9SGG3; -.
DR PaxDb; Q9SGG3; -.
DR PRIDE; Q9SGG3; -.
DR ProteomicsDB; 244828; -.
DR EnsemblPlants; AT1G72700.1; AT1G72700.1; AT1G72700.
DR EnsemblPlants; AT1G72700.2; AT1G72700.2; AT1G72700.
DR EnsemblPlants; AT1G72700.3; AT1G72700.3; AT1G72700.
DR GeneID; 843602; -.
DR Gramene; AT1G72700.1; AT1G72700.1; AT1G72700.
DR Gramene; AT1G72700.2; AT1G72700.2; AT1G72700.
DR Gramene; AT1G72700.3; AT1G72700.3; AT1G72700.
DR KEGG; ath:AT1G72700; -.
DR Araport; AT1G72700; -.
DR TAIR; locus:2030180; AT1G72700.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9SGG3; -.
DR OMA; ETRYWTW; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9SGG3; -.
DR BioCyc; ARA:AT1G72700-MON; -.
DR PRO; PR:Q9SGG3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGG3; baseline and differential.
DR Genevisible; Q9SGG3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0140327; F:flippase activity; IDA:TAIR.
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; -; 2.
DR Gene3D; 3.40.50.1000; -; 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 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; Isopeptide bond; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1228
FT /note="Probable phospholipid-transporting ATPase 5"
FT /id="PRO_0000046389"
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..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..968
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 969..988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1018
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1042..1054
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1055..1077
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1078..1083
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1084..1104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1105..1117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1147..1228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 425
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 879
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SLK6"
SQ SEQUENCE 1228 AA; 139342 MW; 47E47A9297131CB8 CRC64;
MARGRIRSKL RLSLLYTFGC LRPATLEGQD SQPIQGPGFS RTVFCNQPHM HKKKPLRYRS
NYVSTTRYNL ITFFPKSLYE QFHRAANLYF LVAAILSVFP LSPFNKWSMI APLVFVVGLS
MLKEALEDWR RFMQDVKINA RKTCVHKSDG VFRQRKWKKV SVGDIVKVEK DEFFPADLLL
LSSSYEDGIC YVETMNLDGE TNLKVKRSLE VSLPLDDDES FKNFMATIRC EDPNPNLYTF
VGNLEFERQT FPLDPSQILL RDSKLRNTTY VYGVVVFTGF DTKVMQNSTK SPSKRSRIER
TMDYIIYTLL VLLILISCIS SSGFAWETEF HMPKMWYLRP GEPIDFTNPI NPIYAGVVHL
ITALLLYGYL IPISLYVSIE VVKVWQASFI NQDLHMYDDE SGVPANARTS NLNEELGQVH
TILSDKTGTL TCNQMDFLKC SIAGTSYGVR SSEVEVAAAK QMAVDLEEHG EISSTPQSQT
KVYGTWDSSR TQEIEVEGDN NYNTPRAPIK GFGFEDNRLM NGNWLRESQP NDILQFFRIL
AICHTAIPEL NEETGKYTYE AESPDEASFL AAAREFGFEF FKRTQSSVFI RERFSGSGQI
IEREYKVLNL LEFTSKRKRM TVIVRDEEGQ ILLLCKGADS IIFERLAKNG KTYLGPTTRH
LTEYGEAGLR TLALAYRKLD EDEYAAWNSE FLKAKTSIGS DRDELLETGA DMIEKELILI
GATAVEDKLQ KGVPQCIDKL AQAGLKLWVL TGDKMETAIN IGFACSLLRQ GMRQICITSM
NSEGGSQDSK RVVKENILNQ LTKAVQMVKL EKDPHAAFAL IIDGKTLTYA LEDDMKYQFL
ALAVDCASVI CCRVSPKQKA LVVRLVKEGT GKTTLAIGDG ANDVGMIQEA DIGVGISGVE
GMQAVMASDF SIAQFRFLER LLVVHGHWCY KRIAQMICYF FYKNIAFGLT LFYFEAFTGF
SGQSVYNDYY LLLFNVVLTS LPVIALGVFE QDVSSEICLQ FPALYQQGTK NLFFDWSRIL
GWMCNGVYAS LVIFFLNIGI IYSQAFRDNG QTADMDAVGT TMFTCIIWAA NVQIALTMSH
FTWIQHVLIW GSIGMWYLFV AIYSMMPPSY SGNIYRILDE ILAPAPIYWM ATLLVTVAAV
LPYVAHIAFQ RFLNPLDHHI IQEIKYYGRD IEDARLWTRE RTKAREKTKI GFTARVDAKI
RHLRSKLNKK QSNLSHFSAQ DAMSPRSL
