Reviewed, UniProtKB/Swiss-Prot Q9SAF5 (ALA11_ARATH)

Names and origin

Protein names

Recommended name:
    Putative phospholipid-transporting ATPase 11
      Short name=AtALA11
    EC=3.6.3.1
Alternative name(s):
    Aminophospholipid flippase 11

Gene names

Name:	ALA11
Ordered Locus Names:	At1g13210
ORF Names:	F3F19.24

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	1203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in transport of phospholipids Potential.
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.

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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1203	1203	Putative phospholipid-transporting ATPase 11		PRO_0000046395
Regions
	Topological domain	1 – 71	71	Cytoplasmic Potential
	Transmembrane	72 – 93	22	Potential
	Topological domain	94 – 97	4	Extracellular Potential
	Transmembrane	98 – 120	23	Potential
	Topological domain	121 – 303	183	Cytoplasmic Potential
	Transmembrane	304 – 325	22	Potential
	Topological domain	326 – 363	38	Extracellular Potential
	Transmembrane	364 – 381	18	Potential
	Topological domain	382 – 921	540	Cytoplasmic Potential
	Transmembrane	922 – 941	20	Potential
	Topological domain	942 – 955	14	Extracellular Potential
	Transmembrane	956 – 975	20	Potential
	Topological domain	976 – 1005	30	Cytoplasmic Potential
	Transmembrane	1006 – 1028	23	Potential
	Topological domain	1029 – 1041	13	Extracellular Potential
	Transmembrane	1042 – 1064	23	Potential
	Topological domain	1065 – 1070	6	Cytoplasmic Potential
	Transmembrane	1071 – 1091	21	Potential
	Topological domain	1092 – 1108	17	Extracellular Potential
	Transmembrane	1109 – 1133	25	Potential
	Topological domain	1134 – 1203	70	Cytoplasmic Potential
Sites
	Active site	429	1	4-aspartylphosphate intermediate By similarity
	Metal binding	866	1	Magnesium By similarity
	Metal binding	870	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SAF5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D06ED2FBA046FC6E	FASTA	1,203	136,584
	10 20 30 40 50 60 MTKCRRRRLH LSNIYAFKGR KSNFQEDHSH IGGPGFSRVV YCNEPNSPAA ERRNYVGNYV 70 80 90 100 110 120 RSTKYTLASF IPKSLFEQFR RVANFYFLVT GVLSLTALSP YSPISALLPL TFVIAASMVK 130 140 150 160 170 180 EAIEDWGRKK QDIEMNNRKV KVHDGNGIFR REGWRDLKVG NIVRVEKDEF FPADLLLLSS 190 200 210 220 230 240 SYEDSICYVE TMNLDGETNL KVKQGLEATS SALHEDSDFK ELKAVVKCED PNADLYTFVG 250 260 270 280 290 300 TLHFEEQRLP LSITQLLLRD SKLRNTEYIY GVVVFTGHDT KVIQNSTDPP SKRSRIERKM 310 320 330 340 350 360 DKIIYLMFGV VFLMSFIGSI VFGIETREDR VRNGGRTERW YLRPDNADIF FDPDRAPMAA 370 380 390 400 410 420 VYHFFTAVML YSYFIPISLY VSIEIVKVLQ SLFINNDILM YYEENDKPAH ARTSNLNEEL 430 440 450 460 470 480 GMVDTILSDK TGTLTCNSME FIKCSIAGTA YGRGITEVER SMAMRSNGSS LVGDDLDVVV 490 500 510 520 530 540 DQSGPKIKGF NFLDERVMKG NWVKQRDAAV LQKFFRLLAV CHTAIPETDE ATGSVSYEAE 550 560 570 580 590 600 SPDEAAFVVA AREFGFEFFS RTQNGISFRE LDLASGKTVE RVYRLLNVLE FNSARKRMSV 610 620 630 640 650 660 IVRDEDGRLL LLSKGADNVM FERLAKNGRK FEEKTREHVN EYADAGLRTL ILAYREVDEN 670 680 690 700 710 720 EYIEFSKNFN EAKNSVTADR ESLIDEITEQ MERDLILLGA TAVEDKLQNG VPDCIDKLAQ 730 740 750 760 770 780 AGIKIWVLTG DKMETAINIG FACSLLRQEM KQIIINLETP HIKALEKAGE KDAIEHASRE 790 800 810 820 830 840 SVVNQMEEGK ALLTASSSAS SHEAFALIID GKSLTYALED DFKKKFLDLA TGCASVICCR 850 860 870 880 890 900 SSPKQKALVT RLVKSGTGKT TLAIGDGAND VGMLQEADIG VGISGVEGMQ AVMSSDIAIA 910 920 930 940 950 960 QFRYLERLLL VHGHWCYSRI SSMICYFFYK NITFGVTVFL YEAYTSFSAQ PAYNDWFLSL 970 980 990 1000 1010 1020 FNVFFSSLPV IALGVFDQDV SARYCYKFPL LYQEGVQNLL FSWKRIIGWM FNGVFTALAI 1030 1040 1050 1060 1070 1080 FFLCKESLKH QLYNPNGKTA GREILGGTMY TCVVWVVNLQ MALAISYFTW LQHIVIWGSV 1090 1100 1110 1120 1130 1140 AFWYIFLMIY GAITPSFSTD AYKVFIEALA PAPSYWLTTL FVMFFALIPF FVFKSVQMRF 1150 1160 1170 1180 1190 1200 FPGYHQMIQW IRYEGHSNDP EFVEMVRQRS IRPTTVGFTA RRAASVRRSG RFHDQLNKNF IAF

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007357 Genomic DNA. Translation: AAD31074.1. AY099862 mRNA. Translation: AAM20713.1.
IPI	IPI00534449.
PIR	F86266.
RefSeq	NP_172780.1.
UniGene	At.27871
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9SAF5.
Genome annotation databases
GeneID	837881.
GenomeReviews	Gene locus AT1G13210 in contig CT485782_GR.
KEGG	ath:AT1G13210.
NMPDR	fig|3702.1.peg.1590.
Organism-specific databases
TAIR	At1g13210.
Phylogenomic databases
OMA	KEAIEDW.
Enzyme and pathway databases
BRENDA	3.6.3.1. 302.
Gene expression databases
ArrayExpress	Q9SAF5.
Genevestigator	Q9SAF5.
GermOnline	AT1G13210. 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. 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...

Entry information

Entry name

ALA11_ARATH

Accession

Primary (citable) accession number: Q9SAF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)