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Database: UniProt
Entry: ALA5_ARATH
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Original site: 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   27-MAR-2024, entry version 169.
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.Q9SGG3; -.
DR   iPTMnet; Q9SGG3; -.
DR   PaxDb; 3702-AT1G72700-1; -.
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; AT1G72700; ALA5.
DR   eggNOG; KOG0206; Eukaryota.
DR   HOGENOM; CLU_000846_5_2_1; -.
DR   InParanoid; Q9SGG3; -.
DR   OMA; TANEMDF; -.
DR   OrthoDB; 275833at2759; -.
DR   PhylomeDB; Q9SGG3; -.
DR   BioCyc; ARA:AT1G72700-MONOMER; -.
DR   PRO; PR:Q9SGG3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SGG3; baseline and differential.
DR   Genevisible; Q9SGG3; 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:0140327; F:flippase activity; IDA:TAIR.
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; 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; 1.
DR   PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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; 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
//
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