ID ALA1_ARATH Reviewed; 1158 AA.
AC P98204;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Phospholipid-transporting ATPase 1 {ECO:0000303|PubMed:11148289};
DE Short=AtALA1 {ECO:0000303|PubMed:11148289};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 1 {ECO:0000303|PubMed:11402198};
GN Name=ALA1 {ECO:0000303|PubMed:11148289};
GN OrderedLocusNames=At5g04930 {ECO:0000312|Araport:AT5G04930};
GN ORFNames=MUG13.22 {ECO:0000312|EMBL:BAB11515.1};
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 [MRNA], GENE FAMILY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11148289; DOI=10.2307/3871240;
RA Gomes E., Jakobsen M.K., Axelsen K.B., Geisler M., Palmgren M.G.;
RT "Chilling tolerance in Arabidopsis involves ALA1, a member of a new family
RT of putative aminophospholipid translocases.";
RL Plant Cell 12:2441-2454(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=22514601; DOI=10.1371/journal.pone.0033042;
RA Lopez-Marques R.L., Poulsen L.R., Palmgren M.G.;
RT "A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase
RT ALA1, localizes to the plasma membrane following association with a beta-
RT subunit.";
RL PLoS ONE 7:E33042-E33042(2012).
CC -!- FUNCTION: Involved in transport of phospholipids. Contributes to
CC transmembrane flipping of lipids. Has activity with phosphatidylserine
CC and with a much lower efficiency with phosphatidylethanolamine, but not
CC with phosphatidylcholine. {ECO:0000269|PubMed:11148289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:11148289};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22514601}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22514601}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Requires the presence of an ALIS
CC protein to exit the endoplasmic reticulum to the cell membrane.
CC {ECO:0000269|PubMed:22514601}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, anthers, leaves,
CC vascular tissues and stems. {ECO:0000269|PubMed:11148289}.
CC -!- MISCELLANEOUS: Knockdown mutants are cold sensitive.
CC {ECO:0000269|PubMed:11148289}.
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; AF175769; AAG01899.1; -; mRNA.
DR EMBL; AB005245; BAB11515.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90805.1; -; Genomic_DNA.
DR RefSeq; NP_568146.1; NM_120575.3.
DR AlphaFoldDB; P98204; -.
DR SMR; P98204; -.
DR BioGRID; 15654; 4.
DR IntAct; P98204; 2.
DR STRING; 3702.P98204; -.
DR TCDB; 3.A.3.8.7; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P98204; -.
DR PaxDb; 3702-AT5G04930-1; -.
DR ProteomicsDB; 244924; -.
DR EnsemblPlants; AT5G04930.1; AT5G04930.1; AT5G04930.
DR GeneID; 830375; -.
DR Gramene; AT5G04930.1; AT5G04930.1; AT5G04930.
DR KEGG; ath:AT5G04930; -.
DR Araport; AT5G04930; -.
DR TAIR; AT5G04930; ALA1.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; P98204; -.
DR OMA; CDRPDTN; -.
DR OrthoDB; 275833at2759; -.
DR PhylomeDB; P98204; -.
DR BioCyc; ARA:AT5G04930-MONOMER; -.
DR BRENDA; 7.6.2.1; 399.
DR PRO; PR:P98204; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P98204; baseline and differential.
DR Genevisible; P98204; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
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; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF91; 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; SFLDS00003; Haloacid_Dehalogenase; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1158
FT /note="Phospholipid-transporting ATPase 1"
FT /id="PRO_0000046385"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 935..948
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..998
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 999..1020
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1027
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1028..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1056
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1078..1090
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1116..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 859
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 863
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1158 AA; 130329 MW; 5CC042B40C8C974D CRC64;
MDPRKSIDKP PHHDPILGVS SRWSVSSKDN KEVTFGDLGS KRIRHGSAGA DSEMLSMSQK
EIKDEDARLI YINDPDRTNE RFEFTGNSIK TAKYSVFTFL PRNLFEQFHR VAYIYFLVIA
VLNQLPQLAV FGRGASIMPL AFVLLVSAIK DAYEDFRRHR SDRVENNRLA LVFEDHQFRE
KKWKHIRVGE VIKVQSNQTL PCDMVLLATS DPTGVVYVQT TNLDGESNLK TRYAKQETLL
KAADMESFNG FIKCEKPNRN IYGFQANMEI DGRRLSLGPS NIILRGCELK NTAWALGVVV
YAGGETKAML NNSGAPSKRS RLETRMNLEI ILLSLFLIVL CTIAAATAAV WLRTHRDDLD
TILFYRRKDY SERPGGKNYK YYGWGWEIFF TFFMAVIVYQ IMIPISLYIS MELVRIGQAY
FMTNDDQMYD ESSDSSFQCR ALNINEDLGQ IKYLFSDKTG TLTDNKMEFQ CACIEGVDYS
DREPADSEHP GYSIEVDGII LKPKMRVRVD PVLLQLTKTG KATEEAKRAN EFFLSLAACN
TIVPIVSNTS DPNVKLVDYQ GESPDEQALV YAAAAYGFLL IERTSGHIVI NVRGETQRFN
VLGLHEFDSD RKRMSVILGC PDMSVKLFVK GADSSMFGVM DESYGGVIHE TKIQLHAYSS
DGLRTLVVGM RELNDSEFEQ WHSSFEAAST ALIGRAGLLR KVAGNIETNL RIVGATAIED
KLQRGVPEAI ESLRIAGIKV WVLTGDKQET AISIGFSSRL LTRNMRQIVI NSNSLDSCRR
SLEEANASIA SNDESDNVAL IIDGTSLIYV LDNDLEDVLF QVACKCSAIL CCRVAPFQKA
GIVALVKNRT SDMTLAIGDG ANDVSMIQMA DVGVGISGQE GRQAVMASDF AMGQFRFLVP
LLLVHGHWNY QRMGYMILYN FYRNAVFVLI LFWYVLFTCY TLTTAITEWS SVLYSVIYTA
IPTIIIGILD KDLGRQTLLD HPQLYGVGQR AEGYSTTLFW YTMIDTIWQS AAIFFIPMFA
YWGSTIDTSS LGDLWTIAAV VVVNLHLAMD VIRWNWITHA AIWGSIVAAC ICVIVIDVIP
TLPGYWAIFQ VGKTWMFWFC LLAIVVTSLL PRFAIKFLVE YYRPSDVRIA REAEKLGTFR
ESQPVGVEMN LIQDPPRR
//
