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Reviewed, UniProtKB/Swiss-Prot Q9LX20 (ASPL1_ARATH)

Last modified November 3, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Aspartic proteinase-like protein 1
    EC=3.4.23.-
Gene names
Ordered Locus Names: At5g10080
ORF Names: T31P16.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence caution

The sequence BAE98882.1 differs from that shown. Reason: Frameshift at position 145.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentanchored to plasma membrane Ref.3

Inferred from direct assay. Source: TAIR

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 503481Aspartic proteinase-like protein 1
PRO_0000259442
Propeptide504 – 52825Removed in mature form Potential
PRO_0000259443

Regions

Compositional bias155 – 1606Poly-Ser
Compositional bias501 – 51010Poly-Ser
Compositional bias518 – 5214Poly-Leu

Sites

Active site1181 By similarity
Active site3331 By similarity

Amino acid modifications

Lipidation5031GPI-anchor amidated serine Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9LX20-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C1D156857EA7B119

FASTA52857,961
        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

« Hide

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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. expand/collapse author list , 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]"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. expand/collapse author list , 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.
[3]"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.
[4]"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.

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Cross-references

Sequence databases

AL356332 Genomic DNA. Translation: CAB92049.1.
AK226784 mRNA. Translation: BAE98882.1. Frameshift.
IPIIPI00538600.
PIRT50012.
RefSeqNP_196570.1.
UniGeneAt.54796

3D structure databases

HSSPHSSP built from PDB template 1FMX based on UniProtKB P07267.
ModBaseSearch...

Protein family/group databases

MEROPSA01.A55.

Proteomic databases

PRIDEQ9LX20.

Genome annotation databases

GeneID830872.
GenomeReviewsGene locus AT5G10080 in contig BA000015_GR.
KEGGath:AT5G10080.
NMPDRfig|3702.1.peg.23137.

Organism-specific databases

TAIRAt5g10080.

Phylogenomic databases

OMARIFFGDQ

Gene expression databases

GenevestigatorQ9LX20.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameASPL1_ARATH
AccessionPrimary (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: November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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