ALA6_ARATH
ID ALA6_ARATH Reviewed; 1240 AA.
AC Q9SLK6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Phospholipid-transporting ATPase 6 {ECO:0000303|PubMed:11402198};
DE Short=AtALA6 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 6 {ECO:0000303|PubMed:11402198};
GN Name=ALA6 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g54280 {ECO:0000312|Araport:AT1G54280};
GN ORFNames=F20D21.10 {ECO:0000312|EMBL:AAD25608.2};
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).
RN [4]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25954280; DOI=10.3389/fpls.2015.00197;
RA McDowell S.C., Lopez-Marques R.L., Cohen T., Brown E., Rosenberg A.,
RA Palmgren M.G., Harper J.F.;
RT "Loss of the Arabidopsis thaliana P4-ATPases ALA6 and ALA7 impairs pollen
RT fitness and alters the pollen tube plasma membrane.";
RL Front. Plant Sci. 6:197-197(2015).
CC -!- FUNCTION: Involved in transport of phospholipids and in regulation of
CC pollen plasma membrane lipid asymmetry. {ECO:0000305|PubMed:25954280}.
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:0000269|PubMed:25954280};
CC Multi-pass membrane protein {ECO:0000255}. Endomembrane system
CC {ECO:0000269|PubMed:25954280}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Ala6 and ala7 double mutants are hypersensitive
CC to temperature stress and are impaired in pollen fitness with an
CC altered lipid composition and short and slow pollen tubes.
CC {ECO:0000269|PubMed:25954280}.
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=AAD25608.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005287; AAD25608.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33075.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60104.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60105.1; -; Genomic_DNA.
DR PIR; C96584; C96584.
DR RefSeq; NP_001319223.1; NM_001333639.1.
DR RefSeq; NP_001322413.1; NM_001333640.1.
DR RefSeq; NP_175830.1; NM_104306.3.
DR AlphaFoldDB; Q9SLK6; -.
DR SMR; Q9SLK6; -.
DR STRING; 3702.AT1G54280.1; -.
DR iPTMnet; Q9SLK6; -.
DR PaxDb; Q9SLK6; -.
DR PRIDE; Q9SLK6; -.
DR ProteomicsDB; 244900; -.
DR EnsemblPlants; AT1G54280.1; AT1G54280.1; AT1G54280.
DR EnsemblPlants; AT1G54280.2; AT1G54280.2; AT1G54280.
DR EnsemblPlants; AT1G54280.3; AT1G54280.3; AT1G54280.
DR GeneID; 841869; -.
DR Gramene; AT1G54280.1; AT1G54280.1; AT1G54280.
DR Gramene; AT1G54280.2; AT1G54280.2; AT1G54280.
DR Gramene; AT1G54280.3; AT1G54280.3; AT1G54280.
DR KEGG; ath:AT1G54280; -.
DR Araport; AT1G54280; -.
DR TAIR; locus:2020038; AT1G54280.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9SLK6; -.
DR OMA; VQEPFFP; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9SLK6; -.
DR BioCyc; ARA:AT1G54280-MON; -.
DR PRO; PR:Q9SLK6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SLK6; baseline and differential.
DR Genevisible; Q9SLK6; AT.
DR GO; GO:0012505; C:endomembrane system; 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:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:TAIR.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR GO; GO:1905038; P:regulation of membrane lipid metabolic process; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Isopeptide bond; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1240
FT /note="Phospholipid-transporting ATPase 6"
FT /id="PRO_0000046390"
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..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 944..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 964..977
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 998..1027
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1028..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1063
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1064..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1087..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1114..1130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1131..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1156..1240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 426
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 888
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 892
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 1240 AA; 140102 MW; 63866920588AFB9C CRC64;
MARRRIRSRI RKSHFYTFRC LRPKTLDDQG PHVINGPGYT RIVHCNQPHL HLATKLIRYR
SNYVSTTRYN LLTFLPKCLY EQFHRVANFY FLVAAILSVF PLSPFNKWSM IAPLVFVVGL
SMGKEALEDW RRFMQDVEVN SRKASVHKGS GDFGRRTWKR IRVGDIVRVE KDEFFPADLL
LLSSSYEDGI CYVETMNLDG ETNLKVKRCL DATLALEKDE SFQNFSGTIK CEDPNPNLYT
FVGNLECDGQ VYPLDPNQIL LRDSKLRNTA YVYGVVVFTG HDTKVMQNST KSPSKRSRIE
KRMDYIIYTL FALLLTVSFI SSLGFAVMTK LLMAEWWYLR PDKPESLTNP TNPLYAWVVH
LITALLLYGY LIPISLYVSI EVVKVLQAHF INQDLQLYDS ESGTPAQART SNLNEELGQV
DTILSDKTGT LTCNQMDFLK CSIAGTSYGV RASEVELAAA KQMAMDLEEK GEEVANLSMN
KGRTQRYAKL ASKTSSDFEL ETVVTASDEK DQKQNTGVKG FSFEDNRLMN ENWLNEPNSD
DILMFFRILA VCHTAIPEVD EDTGMCTYEA ESPDEVAFLV ASREFGFEFT KRTQSSVFIA
ERFSSSGQPV DREYKILNLL DFTSKRKRMS AIVRDEEGQI LLLCKGADSI IFERLSKSGK
EYLGATSKHL NVYGEAGLRT LALGYRKLDE TEYAAWNSEF HKAKTSVGAD RDEMLEKVSD
MMEKELILVG ATAVEDKLQK GVPQCIDNLA QAGLKIWVLT GDKMETAINI GYACSLLRQG
MKQISISLTN VEESSQNSEA AAKESILMQI TNASQMIKIE KDPHAAFALI IDGKTLTYAL
KDDVKYQFLA LAVDCASVIC CRVSPKQKAL VTRLAKEGTG KTTLAIGDGA NDVGMIQEAD
IGVGISGVEG MQAVMASDFS IAQFRFLERL LVVHGHWCYK RIAQMICYFF YKNITFGLTL
FYFECFTGFS GQSIYNDSYL LLFNVVLTSL PVISLGVFEQ DVPSDVCLQF PALYQQGPKN
LFFDWYRILG WMGNGVYASI VIFTLNLGIF HVQSFRSDGQ TADMNAMGTA MFTCIIWAVN
VQIALTMSHF TWIQHVMIWG SIGAWYVFLA LYGMLPVKLS GNIFHMLVEI LAPAPIFWLT
SLLVIAATTL PYLFHISYQR SVNPLDHHII QEIKHFRIDV EDERMWKREK SKAREKTKIG
FTARVDAKIR QLRGRLQRKH SVLSVMSGTS SNDTPSSNSQ
