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Reviewed, UniProtKB/Swiss-Prot P42210 (ASPR_HORVU)

Last modified February 9, 2010. Version 81. 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:
    Phytepsin
    EC=3.4.23.40
Alternative name(s):
    Aspartic proteinase
Cleaved into the following 4 chains:
    1- Recommended name:
            Phytepsin 32 kDa subunit
    2- Recommended name:
            Phytepsin 29 kDa subunit
    3- Recommended name:
            Phytepsin 16 kDa subunit
    4- Recommended name:
            Phytepsin 11 kDa subunit
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

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Protein attributes

Sequence length508 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)

Catalytic activity

Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.

Subunit structure

Heterodimer of two subunits (29 kDa and 11 kDa) processed from the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an intermediate precursor form.

Subcellular location

Vacuole.

Tissue specificity

Embryo and leaf.

Sequence similarities

Belongs to the peptidase A1 family.

Contains 1 saposin B-type domain.

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Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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
Propeptide23 – 6644Activation peptide
PRO_0000025903
Chain67 – 377311Phytepsin 32 kDa subunit
PRO_0000025904
Chain67 – ?Phytepsin 29 kDa subunitPRO_0000025905
Chain378 – 508131Phytepsin 16 kDa subunit
PRO_0000025906
Chain422 – 50887Phytepsin 11 kDa subunit
PRO_0000025907

Regions

Domain314 – 419106Saposin B-type

Sites

Active site1021
Active site2891
Site377 – 3782Cleavage
Site421 – 4222Cleavage

Amino acid modifications

Glycosylation3991N-linked (GlcNAc...) Potential
Disulfide bond115 ↔ 121
Disulfide bond280 ↔ 284
Disulfide bond427 ↔ 464

Secondary structure

1 ....................................................................................................... 508
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P42210-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 87F2C9F93369B962

FASTA50854,226
        10         20         30         40         50         60 
MGTRGLALAL LAAVLLLQTV LPAASEAEGL VRIALKKRPI DRNSRVATGL SGGEEQPLLS 

        70         80         90        100        110        120 
GANPLRSEEE GDIVALKNYM NAQYFGEIGV GTPPQKFTVI FDTGSSNLWV PSAKCYFSIA 

       130        140        150        160        170        180 
CYLHSRYKAG ASSTYKKNGK PAAIQYGTGS IAGYFSEDSV TVGDLVVKDQ EFIEATKEPG 

       190        200        210        220        230        240 
ITFLVAKFDG ILGLGFKEIS VGKAVPVWYK MIEQGLVSDP VFSFWLNRHV DEGEGGEIIF 

       250        260        270        280        290        300 
GGMDPKHYVG EHTYVPVTQK GYWQFDMGDV LVGGKSTGFC AGGCAAIADS GTSLLAGPTA 

       310        320        330        340        350        360 
IITEINEKIG AAGVVSQECK TIVSQYGQQI LDLLLAETQP KKICSQVGLC TFDGTRGVSA 

       370        380        390        400        410        420 
GIRSVVDDEP VKSNGLRADP MCSACEMAVV WMQNQLAQNK TQDLILDYVN QLCNRLPSPM 

       430        440        450        460        470        480 
GESAVDCGSL GSMPDIEFTI GGKKFALKPE EYILKVGEGA AAQCISGFTA MDIPPPRGPL 

       490        500 
WILGDVFMGP YHTVFDYGKL RIGFAKAA

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References

[1]"Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D."
Runeberg-Roos P., Toermaekangas K., Oestman A.
Eur. J. Biochem. 202:1021-1027(1991) [PubMed: 1722454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Kustaa.
Tissue: Embryo.
[2]"Aspartic proteinase from barley seeds is related to animal cathepsin D."
Toermaekangas K., Runeberg-Roos P., Oestman A., Tilgmann C., Sarkkinen P., Kervinen J., Mikola L., Kalkkinen N.
Adv. Exp. Med. Biol. 306:355-359(1991) [PubMed: 1812727] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Kustaa.
Tissue: Embryo.
[3]"Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting."
Kervinen J., Tobin G.J., Costa J., Waugh D.S., Wlodawer A., Zdanov A.
EMBO J. 18:3947-3955(1999) [PubMed: 10406799] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56136 mRNA. Translation: CAA39602.1.
PIRS19697.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QDMX-ray2.30A/B/C31-508[»]
ModBaseSearch...

Protein family/group databases

MEROPSA01.020.

Organism-specific databases

GrameneP42210.

Enzyme and pathway databases

BRENDA3.4.23.40. 283.

Gene expression databases

GenevestigatorP42210.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
G3DSA:1.10.225.10. Saposin_like. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
PF05184. SapB_1. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SMARTSM00741. SapB. 1 hit.
[Graphical view]
PROSITEPS00141. ASP_PROTEASE. 2 hits.
PS50015. SAP_B. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameASPR_HORVU
AccessionPrimary (citable) accession number: P42210
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 9, 2010
This is version 81 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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