Reviewed, UniProtKB/Swiss-Prot Q9XIE6 (ALA3_ARATH)

Names and origin

Protein names

Recommended name:
    Phospholipid-transporting ATPase 3
      Short name=AtALA3
    EC=3.6.3.1
Alternative name(s):
    Aminophospholipid flippase 3

Gene names

Name:	ALA3
Ordered Locus Names:	At1g59820
ORF Names:	F23H11.14

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Required for secretory processes during plant development. Requires an interaction with ALIS1 for activity. Ref.3
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subunit structure	Associates with ALIS1 to form a stable and active complex. Interacts with ALIS3 and ALIS5 in an heterologous system. Ref.3
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein. Ref.3
Tissue specificity	Expressed in petals and sepals, but not in reproductive tissues. In siliques, detected in the upper part of the seed pod and in the area between the seed pod and the stem, but not in developing seeds. Strong expression in vascular shoot tissues and in stomatal guard cells of young rosettes leaves. In roots, expressed in cells surrounding the xylem and in central and peripheral columella cells. Ref.3
Disruption phenotype	Impaired growth of roots and shoots. Roots devoided of the characteristic trans-golgi proliferation of slime vesicles containing polysaccharides and enzymes for secretion. Ref.3
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.
Sequence caution	The sequence AAD39325.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Golgi apparatus 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 Golgi vesicle budding Ref.3 Inferred from mutant phenotype. Source: TAIR phospholipid transport Inferred from electronic annotation. Source: InterPro root development Ref.3 Inferred from mutant phenotype. Source: TAIR shoot development Ref.3 Inferred from mutant phenotype. Source: TAIR
Cellular component	Golgi apparatus Inferred from direct assay. Source: TAIR 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1213	1213	Phospholipid-transporting ATPase 3		PRO_0000046387
Regions
	Topological domain	1 – 67	67	Cytoplasmic Potential
	Transmembrane	68 – 89	22	Potential
	Topological domain	90 – 93	4	Extracellular Potential
	Transmembrane	94 – 116	23	Potential
	Topological domain	117 – 297	181	Cytoplasmic Potential
	Transmembrane	298 – 319	22	Potential
	Topological domain	320 – 346	27	Extracellular Potential
	Transmembrane	347 – 364	18	Potential
	Topological domain	365 – 900	536	Cytoplasmic Potential
	Transmembrane	901 – 920	20	Potential
	Topological domain	921 – 934	14	Extracellular Potential
	Transmembrane	935 – 954	20	Potential
	Topological domain	955 – 984	30	Cytoplasmic Potential
	Transmembrane	985 – 1006	22	Potential
	Topological domain	1007 – 1013	7	Extracellular Potential
	Transmembrane	1014 – 1036	23	Potential
	Topological domain	1037 – 1042	6	Cytoplasmic Potential
	Transmembrane	1043 – 1063	21	Potential
	Topological domain	1064 – 1076	13	Extracellular Potential
	Transmembrane	1077 – 1087	11	Potential
	Topological domain	1088 – 1213	126	Cytoplasmic Potential
Sites
	Active site	413	1	4-aspartylphosphate intermediate By similarity
	Metal binding	845	1	Magnesium By similarity
	Metal binding	849	1	Magnesium By similarity
Experimental info
	Mutagenesis	413	1	D → A: Loss of internalization of phospholipids. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9XIE6-1 [UniParc]. Last modified February 28, 2003. Version 2. Checksum: 938642DEFDA28B66	FASTA	1,213	137,753
	10 20 30 40 50 60 MVRSGSFSVD SSATHQRTPS RTVTLGHIQP QAPTYRTVYC NDRESNQPVR FKGNSISTTK 70 80 90 100 110 120 YNVFTFLPKG LFEQFRRIAN IYFLGISCLS MTPISPVSPI TNVAPLSMVL LVSLIKEAFE 130 140 150 160 170 180 DWKRFQNDMS INNSTVEILQ DQQWVSIPWR KLQVGDIVKI KKDGFFPADI LFMSSTNSDG 190 200 210 220 230 240 ICYVETANLD GETNLKIRKA LERTWDYLVP EKAYEFKGEI QCEQPNNSLY TFTGNLVVQK 250 260 270 280 290 300 QTLPLSPDQL LLRGCSLRNT EYIVGAVVFT GHETKVMMNA MNAPSKRSTL EKKLDKLIIT 310 320 330 340 350 360 IFCVLVTMCL IGAIGCSIVT DREDKYLGLH NSDWEYRNGL MIGFFTFFTL VTLFSSIIPI 370 380 390 400 410 420 SLYVSIEMIK FIQSTQFINR DLNMYHAETN TPASARTSNL NEELGQVEYI FSDKTGTLTR 430 440 450 460 470 480 NLMEFFKCSI GGVSYGCGVT EIEKGIAQRH GLKVQEEQRS TGAIREKGFN FDDPRLMRGA 490 500 510 520 530 540 WRNEPNPDLC KELFRCLAIC HTVLPEGDES PEKIVYQAAS PDEAALVTAA KNFGFFFYRR 550 560 570 580 590 600 TPTMVYVRES HVEKMGKIQD VAYEILNVLE FNSTRKRQSV VCRFPDGRLV LYCKGADNVI 610 620 630 640 650 660 FERLANGMDD VRKVTREHLE HFGSSGLRTL CLAYKDLNPE TYDSWNEKFI QAKSALRDRE 670 680 690 700 710 720 KKLDEVAELI EKDLILIGST AIEDKLQEGV PTCIETLSRA GIKIWVLTGD KMETAINIAY 730 740 750 760 770 780 ACNLINNEMK QFVISSETDA IREAEERGDQ VEIARVIKEE VKRELKKSLE EAQHSLHTVA 790 800 810 820 830 840 GPKLSLVIDG KCLMYALDPS LRVMLLSLSL NCTSVVCCRV SPLQKAQVTS LVRKGAQKIT 850 860 870 880 890 900 LSIGDGANDV SMIQAAHVGI GISGMEGMQA VMASDFAIAQ FRFLTDLLLV HGRWSYLRIC 910 920 930 940 950 960 KVVMYFFYKN LTFTLTQFWF TFRTGFSGQR FYDDWFQSLF NVVFTALPVI VLGLFEKDVS 970 980 990 1000 1010 1020 ASLSKRYPEL YREGIRNSFF KWRVVAVWAT SAVYQSLVCY LFVTTSSFGA VNSSGKVFGL 1030 1040 1050 1060 1070 1080 WDVSTMVFTC LVIAVNVRIL LMSNSITRWH YITVGGSILA WLVFAFVYCG IMTPHDRNEN 1090 1100 1110 1120 1130 1140 VYFVIYVLMS TFYFYFTLLL VPIVSLLGDF IFQGVERWFF PYDYQIVQEI HRHESDASKA 1150 1160 1170 1180 1190 1200 DQLEVENELT PQEARSYAIS QLPRELSKHT GFAFDSPGYE SFFASQLGIY APQKAWDVAR 1210 RASMRSRPKV PKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"The Arabidopsis P4-ATPase ALA3 localizes to the golgi and requires a beta-subunit to function in lipid translocation and secretory vesicle formation." Poulsen L.R., Lopez-Marques R.L., McDowell S.C., Okkeri J., Licht D., Schulz A., Pomorski T., Harper J.F., Palmgren M.G. Plant Cell 20:658-676(2008) [PubMed: 18344284] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-413, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ALIS1; ALIS3 AND ALIS5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007258 Genomic DNA. Translation: AAD39325.1. Sequence problems. AY091777 mRNA. Translation: AAM10325.1.
IPI	IPI00547552.
PIR	C96622.
RefSeq	NP_176191.1.
UniGene	At.36777
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.8.6. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PRIDE	Q9XIE6.
Genome annotation databases
GeneID	842275.
GenomeReviews	Gene locus AT1G59820 in contig CT485782_GR.
KEGG	ath:AT1G59820.
NMPDR	fig|3702.1.peg.5368.
Organism-specific databases
TAIR	At1g59820.
Enzyme and pathway databases
BRENDA	3.6.3.1. 302.
Gene expression databases
ArrayExpress	Q9XIE6.
Genevestigator	Q9XIE6.
GermOnline	AT1G59820. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 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...

Entry information

Entry name

ALA3_ARATH

Accession

Primary (citable) accession number: Q9XIE6
Secondary accession number(s): Q8RWQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 28, 2003
Last modified:	October 13, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)