Reviewed, UniProtKB/Swiss-Prot Q9S9K4 (ASPL2_ARATH)

Names and origin

Protein names

Recommended name:
    Aspartic proteinase-like protein 2
    EC=3.4.23.-

Gene names

Ordered Locus Names:	At1g65240
ORF Names:	T23K8.15

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	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the peptidase A1 family.
Sequence caution	The sequence AAD26876.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 449	426	Aspartic proteinase-like protein 2
	Propeptide	450 – 475	26	Removed in mature form Potential
Sites
	Active site	92	1	By similarity
	Active site	303	1	By similarity
Amino acid modifications
	Lipidation	449	1	GPI-anchor amidated serine Potential
	Glycosylation	124	1	N-linked (GlcNAc...) Potential
	Glycosylation	222	1	N-linked (GlcNAc...) Potential
	Glycosylation	425	1	N-linked (GlcNAc...) Potential
	Glycosylation	446	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9S9K4-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 1DD9C1A5EF147BA0	FASTA	475	51,828
	10 20 30 40 50 60 MELRRKLCIV VAVFVIVIEF ASANFVFKAQ HKFAGKKKNL EHFKSHDTRR HSRMLASIDL 70 80 90 100 110 120 PLGGDSRVDS VGLYFTKIKL GSPPKEYHVQ VDTGSDILWI NCKPCPKCPT KTNLNFRLSL 130 140 150 160 170 180 FDMNASSTSK KVGCDDDFCS FISQSDSCQP ALGCSYHIVY ADESTSDGKF IRDMLTLEQV 190 200 210 220 230 240 TGDLKTGPLG QEVVFGCGSD QSGQLGNGDS AVDGVMGFGQ SNTSVLSQLA ATGDAKRVFS 250 260 270 280 290 300 HCLDNVKGGG IFAVGVVDSP KVKTTPMVPN QMHYNVMLMG MDVDGTSLDL PRSIVRNGGT 310 320 330 340 350 360 IVDSGTTLAY FPKVLYDSLI ETILARQPVK LHIVEETFQC FSFSTNVDEA FPPVSFEFED 370 380 390 400 410 420 SVKLTVYPHD YLFTLEEELY CFGWQAGGLT TDERSEVILL GDLVLSNKLV VYDLDNEVIG 430 440 450 460 470 WADHNCSSSI KIKDGSGGVY SVGADNLSSA PRLLMITKLL TILSPLIVMA FTSLA

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]

"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment." Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N. J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007230 Genomic DNA. Translation: AAD26876.1. Sequence problems.
PIR	E96676.
RefSeq	NP_176703.1.
UniGene	At.11165
3D structure databases
HSSP	HSSP built from PDB template 1FMX based on UniProtKB P07267.
ModBase	Search...
Genome annotation databases
GeneID	842831.
GenomeReviews	Gene locus AT1G65240 in contig CT485782_GR.
KEGG	ath:AT1G65240.
NMPDR	fig|3702.1.peg.5945.
Organism-specific databases
TAIR	At1g65240.
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. False negative. [Graphical view]
ProDom	Q9S9K4. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ASPL2_ARATH

Accession

Primary (citable) accession number: Q9S9K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	September 2, 2008
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)