ALA2_ARATH
ID ALA2_ARATH Reviewed; 1107 AA.
AC P98205; Q84ME2; Q8W567;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phospholipid-transporting ATPase 2 {ECO:0000303|PubMed:11402198};
DE Short=AtALA2 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid ATPase 2 {ECO:0000303|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 2 {ECO:0000303|PubMed:11402198};
GN Name=ALA2 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At5g44240 {ECO:0000312|Araport:AT5G44240};
GN ORFNames=MLN1.17 {ECO:0000312|EMBL:BAB10991.1};
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 591-1107.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1050, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, MUTAGENESIS OF ASP-381, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH ALIS1; ALIS3 AND ALIS5.
RX PubMed=20053675; DOI=10.1091/mbc.e09-08-0656;
RA Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K.,
RA Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.;
RT "Intracellular targeting signals and lipid specificity determinants of the
RT ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit.";
RL Mol. Biol. Cell 21:791-801(2010).
CC -!- FUNCTION: Involved in transport of phospholipids. Contributes to
CC transmembrane flipping of lipids. Requires an interaction with a
CC protein of the ALIS family for activity. Specific for
CC phosphatidylserine and has no activity with lysolipid,
CC phosphatidylcholine or phosphatidylethanolamine.
CC {ECO:0000269|PubMed:20053675}.
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 -!- SUBUNIT: Interacts with ALIS1, ALIS3 and ALIS5 in a heterologous
CC system. {ECO:0000269|PubMed:20053675}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20053675}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20053675}. Note=Requires the presence of an ALIS
CC protein to exit the endoplasmic reticulum to the prevacuolar
CC compartment. {ECO:0000269|PubMed:20053675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=P98205-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: The intracellular targeting signals and lipid
CC specificity determinants reside in the catalytic ALA subunit.
CC {ECO:0000269|PubMed:20053675}.
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=AAL31943.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB10991.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005239; BAB10991.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95079.1; -; Genomic_DNA.
DR EMBL; AF419611; AAL31943.1; ALT_INIT; mRNA.
DR EMBL; BT006356; AAP21164.1; -; mRNA.
DR RefSeq; NP_001190471.1; NM_001203542.2. [P98205-1]
DR AlphaFoldDB; P98205; -.
DR SMR; P98205; -.
DR BioGRID; 19697; 1.
DR STRING; 3702.AT5G44240.1; -.
DR TCDB; 3.A.3.8.9; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P98205; -.
DR PaxDb; P98205; -.
DR PRIDE; P98205; -.
DR ProteomicsDB; 244812; -. [P98205-1]
DR EnsemblPlants; AT5G44240.2; AT5G44240.2; AT5G44240. [P98205-1]
DR GeneID; 834447; -.
DR Gramene; AT5G44240.2; AT5G44240.2; AT5G44240. [P98205-1]
DR KEGG; ath:AT5G44240; -.
DR Araport; AT5G44240; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; P98205; -.
DR OMA; IAITTWH; -.
DR PhylomeDB; P98205; -.
DR BioCyc; ARA:AT5G44240-MON; -.
DR PRO; PR:P98205; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P98205; baseline and differential.
DR Genevisible; P98205; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1107
FT /note="Phospholipid-transporting ATPase 2"
FT /id="PRO_0000046386"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..807
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..841
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..919
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..982
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 983..1007
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1008..1107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1048..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 381
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 756
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MUTAGEN 381
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20053675"
SQ SEQUENCE 1107 AA; 124836 MW; 31F7729E9653C96F CRC64;
MKRFVYINDD EASKELCCDN RISNRKYTLW NFLPKNLWEQ FSRFMNQYFL LIACLQLWSL
ITPVNPASTW GPLIFIFAVS ASKEAWDDYH RYLSDKKANE KEVWIVKQGI KKHIQAQDIQ
VGNIVWLREN DEVPCDLVLL GTSDPQGVCY VETAALDGET DLKTRVIPSA CVGIDLELLH
KMKGVIECPV PDKDIRRFDA NMRLFPPFID NDVCSLTIKN TLLQSCYLRN TEWACGVSVY
TGNQTKLGMS RGIAEPKLTA MDAMIDKLTG AIFVFQIVVV LVLGIAGNVW KDTEARKQWY
VQYPEEAPWY ELLVIPLRFE LLCSIMIPIS IKVSLDLVKG LYAKFIEWDV EMIDQETGTA
SYAANTAISE DLGQVEYILT DKTGTLTDNK MIFRRCCIGG IFYGNENGDA LKDAQLLNAI
TSGSTDVIRF LTVMAICNTV LPVQSKAGDI VYKAQSQDED ALVIAASKLH MVFVGKNANL
LEIRFNGSVI RYEVLEILEF TSDRKRMSVV VKDCQNGKII LLSKGADEAI LPYARAGQQT
RTIGDAVEHY SQLGLRTLCL AWRELEENEY LEWSVKFKEA SSLLVDREWR IAEVCQRLEH
DLYILGVTAI EDRLQDGVPE TIETLRKAGI NFWMLTGDKQ NTAIQIALSC NFISPEPKGQ
LLMIDGKTEE DVSRSLERVL LTMRITASEP KDVAFVIDGW ALEIALKHHR KDFVELAILS
RTAICCRVTP SQKAQLVEIL KSCDYRTLAI GDGGNDVRMI QQADIGVGIS GREGLQAARA
ADYSIGRFRF LKRLILVHGR YSYNRTAFLS QYSFYKSLLI CFIQIFFSFI SGVSGTSLFN
SVSLMAYNVF YTSVPVLVSV IDKDLSEASV MQHPQILFYC QAGRLLNPST FAGWFGRSLF
HAIIVFVITI HAYAYEKSEM EELGMVALSG CIWLQAFVVA QETNSFTVLQ HLSIWGNLVG
FYAINFLFSA IPSSGMYTIM FRLCSQPSYW ITMFLIVGAG MGPIFALKYF RYTYRPSKIN
ILQQAERMGG PILTLGNIET QPRTIEKDLS PISITQPKNR SPVYEPLLSD SPNATRRSFG
PGTPFEFFQS QSRLSSSSGY TRNCKDN
