Phospholipid-transporting ATPase 1 - Arabidopsis thaliana (Mouse-ear cress)

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Reviewed, UniProtKB/Swiss-Prot P98204 (ALA1_ARATH)

Last modified February 9, 2010. Version 78. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phospholipid-transporting ATPase 1
      Short name=AtALA1
    EC=3.6.3.1
Alternative name(s):
    Aminophospholipid flippase 1

Gene names

Name:	ALA1
Ordered Locus Names:	At5g04930
ORF Names:	MUG13.22

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length	1158 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in transport of phospholipids.
Catalytic activity	ATP + H₂O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

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Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro phospholipid transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: TAIR
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1158

1158

Phospholipid-transporting ATPase 1

PRO_0000046385

Regions

Topological domain

1 – 100

100

Cytoplasmic Potential

Transmembrane

101 – 122

Potential

Topological domain

123 – 127

Extracellular Potential

Transmembrane

128 – 150

Potential

Topological domain

151 – 329

179

Cytoplasmic Potential

Transmembrane

330 – 351

Potential

Topological domain

352 – 391

Extracellular Potential

Transmembrane

392 – 409

Potential

Topological domain

410 – 914

505

Cytoplasmic Potential

Transmembrane

915 – 934

Potential

Topological domain

935 – 948

Extracellular Potential

Transmembrane

949 – 968

Potential

Topological domain

969 – 998

Cytoplasmic Potential

Transmembrane

999 – 1020

Potential

Topological domain

1021 – 1027

Extracellular Potential

Transmembrane

1028 – 1050

Potential

Topological domain

1051 – 1056

Cytoplasmic Potential

Transmembrane

1057 – 1077

Potential

Topological domain

1078 – 1090

Extracellular Potential

Transmembrane

1091 – 1115

Potential

Topological domain

1116 – 1158

Cytoplasmic Potential

Sites

Active site

457

4-aspartylphosphate intermediate By similarity

Metal binding

859

Magnesium By similarity

Metal binding

863

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P98204-1 [UniParc].

Last modified January 11, 2001. Version 1.
Checksum: 5CC042B40C8C974D
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FASTA

1,158

130,329

        10         20         30         40         50         60 
MDPRKSIDKP PHHDPILGVS SRWSVSSKDN KEVTFGDLGS KRIRHGSAGA DSEMLSMSQK 

        70         80         90        100        110        120 
EIKDEDARLI YINDPDRTNE RFEFTGNSIK TAKYSVFTFL PRNLFEQFHR VAYIYFLVIA 

       130        140        150        160        170        180 
VLNQLPQLAV FGRGASIMPL AFVLLVSAIK DAYEDFRRHR SDRVENNRLA LVFEDHQFRE 

       190        200        210        220        230        240 
KKWKHIRVGE VIKVQSNQTL PCDMVLLATS DPTGVVYVQT TNLDGESNLK TRYAKQETLL 

       250        260        270        280        290        300 
KAADMESFNG FIKCEKPNRN IYGFQANMEI DGRRLSLGPS NIILRGCELK NTAWALGVVV 

       310        320        330        340        350        360 
YAGGETKAML NNSGAPSKRS RLETRMNLEI ILLSLFLIVL CTIAAATAAV WLRTHRDDLD 

       370        380        390        400        410        420 
TILFYRRKDY SERPGGKNYK YYGWGWEIFF TFFMAVIVYQ IMIPISLYIS MELVRIGQAY 

       430        440        450        460        470        480 
FMTNDDQMYD ESSDSSFQCR ALNINEDLGQ IKYLFSDKTG TLTDNKMEFQ CACIEGVDYS 

       490        500        510        520        530        540 
DREPADSEHP GYSIEVDGII LKPKMRVRVD PVLLQLTKTG KATEEAKRAN EFFLSLAACN 

       550        560        570        580        590        600 
TIVPIVSNTS DPNVKLVDYQ GESPDEQALV YAAAAYGFLL IERTSGHIVI NVRGETQRFN 

       610        620        630        640        650        660 
VLGLHEFDSD RKRMSVILGC PDMSVKLFVK GADSSMFGVM DESYGGVIHE TKIQLHAYSS 

       670        680        690        700        710        720 
DGLRTLVVGM RELNDSEFEQ WHSSFEAAST ALIGRAGLLR KVAGNIETNL RIVGATAIED 

       730        740        750        760        770        780 
KLQRGVPEAI ESLRIAGIKV WVLTGDKQET AISIGFSSRL LTRNMRQIVI NSNSLDSCRR 

       790        800        810        820        830        840 
SLEEANASIA SNDESDNVAL IIDGTSLIYV LDNDLEDVLF QVACKCSAIL CCRVAPFQKA 

       850        860        870        880        890        900 
GIVALVKNRT SDMTLAIGDG ANDVSMIQMA DVGVGISGQE GRQAVMASDF AMGQFRFLVP 

       910        920        930        940        950        960 
LLLVHGHWNY QRMGYMILYN FYRNAVFVLI LFWYVLFTCY TLTTAITEWS SVLYSVIYTA 

       970        980        990       1000       1010       1020 
IPTIIIGILD KDLGRQTLLD HPQLYGVGQR AEGYSTTLFW YTMIDTIWQS AAIFFIPMFA 

      1030       1040       1050       1060       1070       1080 
YWGSTIDTSS LGDLWTIAAV VVVNLHLAMD VIRWNWITHA AIWGSIVAAC ICVIVIDVIP 

      1090       1100       1110       1120       1130       1140 
TLPGYWAIFQ VGKTWMFWFC LLAIVVTSLL PRFAIKFLVE YYRPSDVRIA REAEKLGTFR 

      1150 
ESQPVGVEMN LIQDPPRR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases." Gomes E., Jakobsen M.K., Axelsen K.B., Geisler M., Palmgren M.G. Plant Cell 12:2441-2454(2000) [PubMed: 11148289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 9330910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF175769 mRNA. Translation: AAG01899.1. AB005245 Genomic DNA. Translation: BAB11515.1.
IPI	IPI00524087.
RefSeq	NP_568146.1.
UniGene	At.21675
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P98204.
Protein family/group databases
TCDB	3.A.3.8.7. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PRIDE	P98204.
ProMEX	P98204.
Genome annotation databases
GeneID	830375.
GenomeReviews	Gene locus AT5G04930 in contig BA000015_GR.
KEGG	ath:AT5G04930.
NMPDR	fig\|3702.1.peg.22591.
Organism-specific databases
TAIR	At5g04930.
Phylogenomic databases
eggNOG	KOG0206.
HOGENOM	HBG745019.
InParanoid	P98204.
OMA	YFIVTLA.
PhylomeDB	P98204.
Enzyme and pathway databases
BRENDA	3.6.3.1. 302.
Gene expression databases
ArrayExpress	P98204.
Genevestigator	P98204.
GermOnline	AT5G04930. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR005834. Dehalogen-like_hydro. IPR013200. HAD-SF_hydro-like_3. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. PF08282. Hydrolase_3. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ALA1_ARATH

Accession

Primary (citable) accession number: P98204

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	February 9, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents