ALA8_ARATH
ID ALA8_ARATH Reviewed; 1189 AA.
AC Q9LK90;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable phospholipid-transporting ATPase 8 {ECO:0000303|PubMed:11402198};
DE Short=AtALA8 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 8 {ECO:0000303|PubMed:11402198};
GN Name=ALA8 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At3g27870 {ECO:0000312|Araport:AT3G27870};
GN ORFNames=K16N12.9 {ECO:0000312|EMBL:BAB02533.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 ---------------------------------------------------------------------------
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; AP000371; BAB02533.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77374.1; -; Genomic_DNA.
DR RefSeq; NP_189425.2; NM_113703.3.
DR AlphaFoldDB; Q9LK90; -.
DR SMR; Q9LK90; -.
DR STRING; 3702.AT3G27870.1; -.
DR iPTMnet; Q9LK90; -.
DR PaxDb; Q9LK90; -.
DR PRIDE; Q9LK90; -.
DR EnsemblPlants; AT3G27870.1; AT3G27870.1; AT3G27870.
DR GeneID; 822407; -.
DR Gramene; AT3G27870.1; AT3G27870.1; AT3G27870.
DR KEGG; ath:AT3G27870; -.
DR Araport; AT3G27870; -.
DR TAIR; locus:2086465; AT3G27870.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q9LK90; -.
DR OMA; PECIHKL; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9LK90; -.
DR BioCyc; ARA:AT3G27870-MON; -.
DR PRO; PR:Q9LK90; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK90; baseline and differential.
DR Genevisible; Q9LK90; 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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1189
FT /note="Probable phospholipid-transporting ATPase 8"
FT /id="PRO_0000046392"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..954
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1040
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1041..1063
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1064..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1133..1189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 424
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 865
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 869
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1189 AA; 135309 MW; DCF951CF3FC55E83 CRC64;
MAGERRKGMK FSKLYSFKCF KPFSREDHSQ IGSRGYSRVV FCNDPDNPEA LQLNYRGNYV
STTKYTAANF IPKSLFEQFR RVANIYFLVV AFVSFSPLAP YTAPSVLAPL LIVIGATMVK
EGVEDLRRRK QDVEANNRKV EVLGKTGTFV ETKWKNLRVG DLVKVHKDEY FPADLLLLSS
SYEDGICYVE TMNLDGETNL KLKHALEITS DEESIKNFRG MIKCEDPNEH LYSFVGTLYF
EGKQYPLSPQ QILLRDSKLK NTDYVYGVVV FTGHDTKVMQ NATDPPSKRS KIEKKMDQII
YILFSILIVI AFTGSVFFGI ATRRDMSDNG KLRRWYLRPD HTTVFYDPRR AVAAAFFHFL
TALMLYGYLI PISLYVSIEV VKVLQSIFIN QDQEMYHEET DRPARARTSN LNEELGQVDT
ILSDKTGTLT CNSMEFVKCS IAGTAYGRGM TEVEVALRKQ KGLMTQEEVG DNESLSIKEQ
KAVKGFNFWD ERIVDGQWIN QPNAELIQKF FRVLAICHTA IPDVNSDTGE ITYEAESPDE
AAFVIASREL GFEFFSRSQT SISLHEIDHM TGEKVDRVYE LLHVLEFSSS RKRMSVIVRN
PENRLLLLSK GADSVMFKRL AKHGRQNERE TKEHIKKYAE AGLRTLVITY REIDEDEYIV
WEEEFLNAKT LVTEDRDALI DAAADKIEKD LILLGSTAVE DKLQKGVPDC IEKLSQAGVK
IWVLTGDKTE TAINIGYACS LLREGMKQIL VTLDSSDIEA LEKQGDKEAV AKASFQSIKK
QLREGMSQTA AVTDNSAKEN SEMFGLVIDG KSLTYALDSK LEKEFLELAI RCNSVICCRS
SPKQKALVTR LVKNGTGRTT LAIGDGANDV GMLQEADIGV GISGAEGMQA VMASDFAIAQ
FRFLERLLLV HGHWCYRRIT LMICYFFYKN LAFGFTLFWY EAYASFSGKP AYNDWYMSCY
NVFFTSLPVI ALGVFDQDVS ARLCLKYPLL YQEGVQNVLF SWERILGWML NGVISSMIIF
FLTINTMATQ AFRKDGQVVD YSVLGVTMYS SVVWTVNCQM AISINYFTWI QHCFIWGSIG
VWYLFLVIYG SLPPTFSTTA FQVFVETSAP SPIYWLVLFL VVFSALLPYF TYRAFQIKFR
PMYHDIIVEQ RRTERTETAP NAVLGELPVQ VEFTLHHLRA NLSRRDSWN
