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Reviewed, UniProtKB/Swiss-Prot O04057 (ASPR_CUCPE)

Last modified July 22, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Aspartic proteinase
    EC=3.4.23.-
OrganismCucurbita pepo (Vegetable marrow) (Summer squash)
Taxonomic identifier3663 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids ICucurbitalesCucurbitaceaeCucurbita

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.

Subunit structure

Heterodimer of a 32 kDa subunit and a 16 kDa subunit.

Subcellular location

Vacuole.

Sequence similarities

Belongs to the peptidase A1 family.

Contains 1 saposin B-type domain.

Ontologies

Keywords

   Cellular componentVacuole
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
Zymogen

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – ?Activation peptide Potential
Chain? – 513Aspartic proteinase

Regions

Domain319 – 424106Saposin B-type

Sites

Active site1081 By similarity
Active site2941 By similarity

Amino acid modifications

Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Disulfide bond120 ↔ 126 By similarity
Disulfide bond285 ↔ 289 By similarity
Disulfide bond432 ↔ 469 By similarity

Sequences

Sequence LengthMass (Da)Tools
O04057-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 083FB7064CE02DC2

FASTA51355,856
        10         20         30         40         50         60 
MASYHSKAAF LCLFLLVSFN IVSSASNDGL LRVGLKKIKL DPENRLAARV ESKDAEILKA 

        70         80         90        100        110        120 
AFRKYNPKGN LGESSDTDIV ALKNYLDAQY YGEIAIGTPP QKFTVIFDTG SSNLWVLCEC 

       130        140        150        160        170        180 
LFSVACHFHA RYKSSRSSSY KKNGTSASIR YGTGAVSGFF SYDNVKVGDL VVKEQVFIEA 

       190        200        210        220        230        240 
TREPSLTFLV AKFDGLLGLG FQEIAVGNAV PVWYNMVEQG LVKEPVFSFW LNRNVEEEEG 

       250        260        270        280        290        300 
GEIVFGGVDP KHYRGKHTYV PVTQKGYWQF DMGDVLIDGE PTGFCDGGCS AIADSGTSLL 

       310        320        330        340        350        360 
AGPTPVITMI NHAIGAKGVV SQQCKAVVAQ YGQTIMDLLL SEADPKKICS QINLCTFDGT 

       370        380        390        400        410        420 
RGVSMGIESV VDENAGKSSD SLHDGMCSVC EMTVVWMQNQ LRQNQTKERI INYINELCDR 

       430        440        450        460        470        480 
MPSPMGQSAV DCGQLSSMPT VSFTIGGKIF DLAPEEYILK VGEGPVAQCI SGFTAFDIPP 

       490        500        510 
PRGPLWILGD VFMGRYHTVF DFGKLRVGSA EAA 

« Hide

References

[1]"An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles of plants."
Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I.
Eur. J. Biochem. 246:133-141(1997) [PubMed: 9210475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AB002695 mRNA. Translation: BAA19607.1.
PIRT09739.

3D structure databases

HSSPHSSP built from PDB template 1QDM based on UniProtKB P42210.
SMRO04057. Positions 54-513.
ModBaseSearch...

Protein family/group databases

MEROPSA01.020.

Family and domain databases

InterProIPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
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.
PR01797. SAPOSIN.
ProDomPD001732. SapB_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00741. SapB. 1 hit.
[Graphical view]
PROSITEPS00141. ASP_PROTEASE. 2 hits.
PS50015. SAP_B. 2 hits.
[Graphical view]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameASPR_CUCPE
AccessionPrimary (citable) accession number: O04057
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 22, 2008
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

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