Q9LX20 (ASPL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartic proteinase-like protein 1
EC=3.4.23.-

Gene names

Ordered Locus Names:	At5g10080
ORF Names:	T31P16.70

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	528 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 Ref.4 Ref.5.
Sequence similarities	Belongs to the peptidase A1 family.
Sequence caution	The sequence BAE98882.1 differs from that shown. Reason: Frameshift at position 145.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to plasma membrane Inferred from direct assay Ref.4. Source: TAIR
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 503	481	Aspartic proteinase-like protein 1		PRO_0000259442
	Propeptide	504 – 528	25	Removed in mature form Potential		PRO_0000259443
Regions
	Compositional bias	155 – 160	6	Poly-Ser
	Compositional bias	501 – 510	10	Poly-Ser
	Compositional bias	518 – 521	4	Poly-Leu
Sites
	Active site	118	1	By similarity
	Active site	333	1	By similarity
Amino acid modifications
	Lipidation	503	1	GPI-anchor amidated serine Potential
	Glycosylation	193	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	358	1	N-linked (GlcNAc...) Potential
	Glycosylation	391	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9LX20 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C1D156857EA7B119	FASTA	528	57,961
	10 20 30 40 50 60 MVSRSAFLLF CVLFLATEET LASLFSSRLI HRFSDEGRAS IKTPSSSDSL PNKQSLEYYR 70 80 90 100 110 120 LLAESDFRRQ RMNLGAKVQS LVPSEGSKTI SSGNDFGWLH YTWIDIGTPS VSFLVALDTG 130 140 150 160 170 180 SNLLWIPCNC VQCAPLTSTY YSSLATKDLN EYNPSSSSTS KVFLCSHKLC DSASDCESPK 190 200 210 220 230 240 EQCPYTVNYL SGNTSSSGLL VEDILHLTYN TNNRLMNGSS SVKARVVIGC GKKQSGDYLD 250 260 270 280 290 300 GVAPDGLMGL GPAEISVPSF LSKAGLMRNS FSLCFDEEDS GRIYFGDMGP SIQQSTPFLQ 310 320 330 340 350 360 LDNNKYSGYI VGVEACCIGN SCLKQTSFTT FIDSGQSFTY LPEEIYRKVA LEIDRHINAT 370 380 390 400 410 420 SKNFEGVSWE YCYESSAEPK VPAIKLKFSH NNTFVIHKPL FVFQQSQGLV QFCLPISPSG 430 440 450 460 470 480 QEGIGSIGQN YMRGYRMVFD RENMKLGWSP SKCQEDKIEP PQASPGSTSS PNPLPTDEQQ 490 500 510 520 SRGGHAVSPA IAGKTPSKTP SSSSSYSFSS IMRLFNSLLL LHWLASLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins." Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N. Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL356332 Genomic DNA. Translation: CAB92049.1. CP002688 Genomic DNA. Translation: AED91491.1. AK226784 mRNA. Translation: BAE98882.1. Frameshift.
IPI	IPI00538600.
PIR	T50012.
RefSeq	NP_196570.1. NM_121046.1.
UniGene	At.54796.
3D structure databases
HSSP	HSSP built from PDB template 1FMX based on UniProtKB P07267.
ProteinModelPortal	Q9LX20.
SMR	Q9LX20. Positions 86-208.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LX20.
Protein family/group databases
MEROPS	A01.A55.
Proteomic databases
PRIDE	Q9LX20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G10080.1; AT5G10080.1; AT5G10080.
GeneID	830872.
GenomeReviews	Gene locus AT5G10080 in contig BA000015_GR.
KEGG	ath:AT5G10080.
NMPDR	fig|3702.1.peg.23137.
Organism-specific databases
TAIR	At5g10080.
Phylogenomic databases
eggNOG	KOG1339.
GeneTree	EPGT00070000028458.
HOGENOM	HBG317990.
InParanoid	Q9LX20.
OMA	VAPDGLM.
PhylomeDB	Q9LX20.
ProtClustDB	CLSN2686359.
Gene expression databases
Genevestigator	Q9LX20.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [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.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPL1_ARATH

Accession

Primary (citable) accession number: Q9LX20
Secondary accession number(s): Q0WVG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program