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P85137 (CARDF_CYNCA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cardosin-F
EC=3.4.23.-

Cleaved into the following 2 chains:

  1. Cardosin-F heavy chain
  2. Cardosin-F light chain
OrganismCynara cardunculus (Cardoon)
Taxonomic identifier4265 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Carduoideae › Cardueae › Carduinae › Cynara

Protein attributes

Sequence length281 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aspartic protease with a high preference for bonds between hydrophobic residues. Ref.1

Enzyme regulation

Inhibited by pepstatin. Ref.1

Subunit structure

Heterodimer of a light chain and a heavy chain. An intermediate form is produced first, and undergoes proteolytic processing to remove the internal plant-specific insert (PSI) and the propeptide. Ref.1 UniProtKB Q9XFX3

Subcellular location

Microsome membrane By similarity. Protein storage vacuole By similarity. Secreted › cell wall By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Procardosin-F is associated with the microsomal membranes, the mature form is secreted By similarity. UniProtKB Q9XFX3

Tissue specificity

Pistils. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

pH dependence:

Optimim pH is 4.3. Active from pH 3 to 6.5. Ref.1

Mass spectrometry

Molecular mass is 27356 Da from positions 1 - ?. Determined by ESI. Heavy chain. Ref.1

Molecular mass is 10778 Da . Determined by ESI. Light chain. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Cardosin-F heavy chain Ref.1PRO_0000286870
Chain? – ›281Cardosin-F light chain Ref.1PRO_0000394453

Sites

Active site361 By similarity UniProtKB P42210
Active site1901 By similarity UniProtKB P42210

Amino acid modifications

Glycosylation2131N-linked (GlcNAc...) Potential
Disulfide bond181 ↔ 185 By similarity UniProtKB P42210
Disulfide bond? ↔ 238 By similarity UniProtKB P42210

Experimental info

Non-adjacent residues48 – 492
Non-adjacent residues62 – 632
Non-adjacent residues214 – 2152
Non-adjacent residues220 – 2212
Non-adjacent residues232 – 2332
Non-terminal residue2811

Sequences

Sequence LengthMass (Da)Tools
P85137 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 865F892032416936

FASTA28130,561
        10         20         30         40         50         60 
ADSGSAVVAL TNDRDTSYYG EIGIGTPPQK FTVIFDTGSS VLWVPSSKAH SMYESSGSST 

        70         80         90        100        110        120 
YKSQDSVTIG DLVVKEQDFI EATEEADNVF LNRLFDGILG LSFQTISVPV WYNMLNQGLV 

       130        140        150        160        170        180 
KRFSFWLNRN VDEEEGGELV FGGLDPNHFR GDHTYVPVTY QYYWQFGIGD VLIGDKSTGF 

       190        200        210        220        230        240 
CAPGCQAFAD SGTSLLSGPT AIVTQINHAI GANGSEELNV KFGLTPEQYI LKGEATQCIS 

       250        260        270        280 
GFTAMDATLL GPLWILGDVF MRPYHTVFDY GNLLVGFAEA A

« Hide

References

[1]"Multiplicity of aspartic proteinases from Cynara cardunculus L."
Sarmento A.C., Lopes H., Oliveira C.S., Vitorino R., Samyn B., Sergeant K., Debyser G., Van Beeumen J., Domingues P., Amado F., Pires E., Domingues M.R., Barros M.T.
Planta 230:429-439(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION, MASS SPECTROMETRY.
Strain: cv. Sylvestris.
Tissue: Stigma.

Cross-references

3D structure databases

ProteinModelPortalP85137.
SMRP85137. Positions 4-213, 221-281.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 2 hits.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
PS50015. SAP_B. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARDF_CYNCA
AccessionPrimary (citable) accession number: P85137
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: March 6, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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