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Protein

Phospholipid-transporting ATPase 2

Gene

ALA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Requires an interaction with a protein of the ALIS family for activity. Specific for phosphatidylserine and has no activity with lysolipid, phosphatidylcholine or phosphatidylethanolamine.1 Publication

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei381 – 38114-aspartylphosphate intermediateBy similarity
Metal bindingi752 – 7521MagnesiumBy similarity
Metal bindingi756 – 7561MagnesiumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G44240-MONOMER.
ARA:GQT-64-MONOMER.

Protein family/group databases

TCDBi3.A.3.8.9. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase 21 Publication (EC:3.6.3.11 Publication)
Short name:
AtALA21 Publication
Alternative name(s):
Aminophospholipid ATPase 21 Publication
Aminophospholipid flippase 21 Publication
Gene namesi
Name:ALA21 Publication
Ordered Locus Names:At5g44240Imported
ORF Names:MLN1.17Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G44240.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicSequence analysisAdd
BLAST
Transmembranei34 – 5522HelicalSequence analysisAdd
BLAST
Topological domaini56 – 605ExtracellularSequence analysis
Transmembranei61 – 8323HelicalSequence analysisAdd
BLAST
Topological domaini84 – 268185CytoplasmicSequence analysisAdd
BLAST
Transmembranei269 – 29022HelicalSequence analysisAdd
BLAST
Topological domaini291 – 31525ExtracellularSequence analysisAdd
BLAST
Transmembranei316 – 33318HelicalSequence analysisAdd
BLAST
Topological domaini334 – 807474CytoplasmicSequence analysisAdd
BLAST
Transmembranei808 – 82720HelicalSequence analysisAdd
BLAST
Topological domaini828 – 84114ExtracellularSequence analysisAdd
BLAST
Transmembranei842 – 86019HelicalSequence analysisAdd
BLAST
Topological domaini861 – 89030CytoplasmicSequence analysisAdd
BLAST
Transmembranei891 – 91222HelicalSequence analysisAdd
BLAST
Topological domaini913 – 9197ExtracellularSequence analysis
Transmembranei920 – 94223HelicalSequence analysisAdd
BLAST
Topological domaini943 – 9486CytoplasmicSequence analysis
Transmembranei949 – 96921HelicalSequence analysisAdd
BLAST
Topological domaini970 – 98213ExtracellularSequence analysisAdd
BLAST
Transmembranei983 – 100725HelicalSequence analysisAdd
BLAST
Topological domaini1008 – 1107100CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi381 – 3811D → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11071107Phospholipid-transporting ATPase 2PRO_0000046386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1050 – 10501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP98205.
PRIDEiP98205.

PTM databases

iPTMnetiP98205.

Expressioni

Gene expression databases

ExpressionAtlasiP98205. baseline and differential.
GenevisibleiP98205. AT.

Interactioni

Subunit structurei

Interacts with ALIS1, ALIS3 and ALIS5 in a heterologous system.1 Publication

Protein-protein interaction databases

BioGridi19697. 1 interaction.
STRINGi3702.AT5G44240.1.

Structurei

3D structure databases

ProteinModelPortaliP98205.
SMRiP98205. Positions 101-782.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ITKD. Eukaryota.
ENOG410XPYK. LUCA.
HOGENOMiHOG000202528.
InParanoidiP98205.
KOiK01530.
PhylomeDBiP98205.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.Curated

Isoform 1 (identifier: P98205-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKRFVYINDD EASKELCCDN RISNRKYTLW NFLPKNLWEQ FSRFMNQYFL
60 70 80 90 100
LIACLQLWSL ITPVNPASTW GPLIFIFAVS ASKEAWDDYH RYLSDKKANE
110 120 130 140 150
KEVWIVKQGI KKHIQAQDIQ VGNIVWLREN DEVPCDLVLL GTSDPQGVCY
160 170 180 190 200
VETAALDGET DLKTRVIPSA CVGIDLELLH KMKGVIECPV PDKDIRRFDA
210 220 230 240 250
NMRLFPPFID NDVCSLTIKN TLLQSCYLRN TEWACGVSVY TGNQTKLGMS
260 270 280 290 300
RGIAEPKLTA MDAMIDKLTG AIFVFQIVVV LVLGIAGNVW KDTEARKQWY
310 320 330 340 350
VQYPEEAPWY ELLVIPLRFE LLCSIMIPIS IKVSLDLVKG LYAKFIEWDV
360 370 380 390 400
EMIDQETGTA SYAANTAISE DLGQVEYILT DKTGTLTDNK MIFRRCCIGG
410 420 430 440 450
IFYGNENGDA LKDAQLLNAI TSGSTDVIRF LTVMAICNTV LPVQSKAGDI
460 470 480 490 500
VYKAQSQDED ALVIAASKLH MVFVGKNANL LEIRFNGSVI RYEVLEILEF
510 520 530 540 550
TSDRKRMSVV VKDCQNGKII LLSKGADEAI LPYARAGQQT RTIGDAVEHY
560 570 580 590 600
SQLGLRTLCL AWRELEENEY LEWSVKFKEA SSLLVDREWR IAEVCQRLEH
610 620 630 640 650
DLYILGVTAI EDRLQDGVPE TIETLRKAGI NFWMLTGDKQ NTAIQIALSC
660 670 680 690 700
NFISPEPKGQ LLMIDGKTEE DVSRSLERVL LTMRITASEP KDVAFVIDGW
710 720 730 740 750
ALEIALKHHR KDFVELAILS RTAICCRVTP SQKAQLVEIL KSCDYRTLAI
760 770 780 790 800
GDGGNDVRMI QQADIGVGIS GREGLQAARA ADYSIGRFRF LKRLILVHGR
810 820 830 840 850
YSYNRTAFLS QYSFYKSLLI CFIQIFFSFI SGVSGTSLFN SVSLMAYNVF
860 870 880 890 900
YTSVPVLVSV IDKDLSEASV MQHPQILFYC QAGRLLNPST FAGWFGRSLF
910 920 930 940 950
HAIIVFVITI HAYAYEKSEM EELGMVALSG CIWLQAFVVA QETNSFTVLQ
960 970 980 990 1000
HLSIWGNLVG FYAINFLFSA IPSSGMYTIM FRLCSQPSYW ITMFLIVGAG
1010 1020 1030 1040 1050
MGPIFALKYF RYTYRPSKIN ILQQAERMGG PILTLGNIET QPRTIEKDLS
1060 1070 1080 1090 1100
PISITQPKNR SPVYEPLLSD SPNATRRSFG PGTPFEFFQS QSRLSSSSGY

TRNCKDN
Length:1,107
Mass (Da):124,836
Last modified:January 11, 2001 - v1
Checksum:i31F7729E9653C96F
GO

Sequence cautioni

The sequence AAL31943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB10991.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005239 Genomic DNA. Translation: BAB10991.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95079.1.
AF419611 mRNA. Translation: AAL31943.1. Different initiation.
BT006356 mRNA. Translation: AAP21164.1.
RefSeqiNP_001190471.1. NM_001203542.1. [P98205-1]
UniGeneiAt.24522.

Genome annotation databases

EnsemblPlantsiAT5G44240.2; AT5G44240.2; AT5G44240. [P98205-1]
GeneIDi834447.
KEGGiath:AT5G44240.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005239 Genomic DNA. Translation: BAB10991.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95079.1.
AF419611 mRNA. Translation: AAL31943.1. Different initiation.
BT006356 mRNA. Translation: AAP21164.1.
RefSeqiNP_001190471.1. NM_001203542.1. [P98205-1]
UniGeneiAt.24522.

3D structure databases

ProteinModelPortaliP98205.
SMRiP98205. Positions 101-782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19697. 1 interaction.
STRINGi3702.AT5G44240.1.

Protein family/group databases

TCDBi3.A.3.8.9. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiP98205.

Proteomic databases

PaxDbiP98205.
PRIDEiP98205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G44240.2; AT5G44240.2; AT5G44240. [P98205-1]
GeneIDi834447.
KEGGiath:AT5G44240.

Organism-specific databases

TAIRiAT5G44240.

Phylogenomic databases

eggNOGiENOG410ITKD. Eukaryota.
ENOG410XPYK. LUCA.
HOGENOMiHOG000202528.
InParanoidiP98205.
KOiK01530.
PhylomeDBiP98205.

Enzyme and pathway databases

BioCyciARA:AT5G44240-MONOMER.
ARA:GQT-64-MONOMER.

Miscellaneous databases

PROiP98205.

Gene expression databases

ExpressionAtlasiP98205. baseline and differential.
GenevisibleiP98205. AT.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
    Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
    DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 591-1107.
    Strain: cv. Columbia.
  4. "Inventory of the superfamily of P-type ion pumps in Arabidopsis."
    Axelsen K.B., Palmgren M.G.
    Plant Physiol. 126:696-706(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  5. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  6. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit."
    Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K., Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.
    Mol. Biol. Cell 21:791-801(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-381, SUBCELLULAR LOCATION, INTERACTION WITH ALIS1; ALIS3 AND ALIS5.

Entry informationi

Entry nameiALA2_ARATH
AccessioniPrimary (citable) accession number: P98205
Secondary accession number(s): Q84ME2, Q8W567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The intracellular targeting signals and lipid specificity determinants reside in the catalytic ALA subunit.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.