Reviewed, UniProtKB/Swiss-Prot P85136 (CARDE_CYNCA)

Names and origin

Protein names	Recommended name:     Cardosin-E     EC=3.4.23.-
Organism	Cynara cardunculus (Cardoon)
Taxonomic identifier	4265 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Carduoideae › Cardueae › Cynara

Protein attributes

Sequence length	224 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Aspartic protease with a high preference for hydrophobic residues.
Subunit structure	Heterodimer of a light chain and a heavy chain.
Tissue specificity	Pistils.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	Kinetic parameters: KM=0.64 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu pH dependence: Optimim pH is 4.4. Active from pH 3 to 6.5.
Mass spectrometry	Molecular weight is 27669 Da . Determined by ESI. Heavy chain. Molecular weight is 10691 Da . Determined by ESI. Light chain.

Ontologies

Keywords
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – ›224	›224	Cardosin-E
Sites
	Active site	35	1	By similarity
	Active site	134	1	By similarity
Amino acid modifications
	Disulfide bond	125 ↔ 129		By similarity
	Disulfide bond	? ↔ 181		By similarity
Experimental info
	Non-adjacent residues	47 – 48	2
	Non-adjacent residues	65 – 66	2
	Non-adjacent residues	157 – 158	2
	Non-adjacent residues	163 – 164	2
	Non-adjacent residues	175 – 176	2
	Non-terminal residue	224	1

Sequences

	Sequence		Length	Mass (Da)
	P85136-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 2A72113B52B60DFA	FASTA	224	24,507
	10 20 30 40 50 60 DSGSAIVALT NDRDTSYFGE IGIGTPPQKY TVIYDTGSSV LWVPSSKEQD FIEATDETDN 70 80 90 100 110 120 VFLHRRFSFW LNRNVDEEEG GELVFGGLDP NHFRGDHTYV PVTYQYYWQF GIGDVLIGDK 130 140 150 160 170 180 STGFCAPGCQ AFADSGTSLL SGPTAIVTQI NHAIGANSEE LNVKFGLTPE QYILKGEATQ 190 200 210 220 CISGFTAMDA TLLGPLWILG DVFMRPYHTV FDYGNLLVGF AEAA

References

[1]

"Multiple floral aspartic proteinases in Cynara cardunculus subsp. flavescens." Sarmento A.C., Pires E., Barros M. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION, MASS SPECTROMETRY. Strain: cv. Sylvestris. Tissue: Pistil.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. IPR008139. SaposinB. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. Partial match. PS50015. SAP_B. Partial match. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CARDE_CYNCA

Accession

Primary (citable) accession number: P85136

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 15, 2007
Last modified:	July 22, 2008
This is version 7 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)