Reviewed, UniProtKB/Swiss-Prot P85139 (CARDH_CYNCA)

Names and origin

Protein names	Recommended name:     Cardosin-H     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	265 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	pH dependence: Optimum pH is 4.3. Active from pH 3 to pH 7.0.
Mass spectrometry	Molecular weight is 27134 Da . Determined by ESI. Heavy chain Molecular weight is 10778 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 – ›265	›265	Cardosin-H
Sites
	Active site	35	1	By similarity
	Active site	176	1	By similarity
Amino acid modifications
	Disulfide bond	167 ↔ 171		By similarity
	Disulfide bond	? ↔ 222		By similarity
Experimental info
	Non-adjacent residues	47 – 48	2
	Non-adjacent residues	61 – 62	2
	Non-adjacent residues	107 – 108	2
	Non-adjacent residues	199 – 200	2
	Non-adjacent residues	205 – 206	2
	Non-adjacent residues	216 – 217	2
	Non-terminal residue	265	1

Sequences

	Sequence		Length	Mass (Da)
	P85139-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 001A9E5CC81D2F2D	FASTA	265	28,985
	10 20 30 40 50 60 DSGSAVVALT NDRDTSYFGE IGIGTPPQKF TVIFDTGSSV LWVPSSKAHS MYESSGSSTY 70 80 90 100 110 120 KEQDFIEATD ETDNVFLHRL FDGILGLSFQ TISVPVWYNM LNQGLVKRFS FWLNRNVDEE 130 140 150 160 170 180 EGGELVFGGL DPNHFRGDHT YVPVTYQYYW QFGIGDVLIG DKSTGFCAPG CQAFADSGTS 190 200 210 220 230 240 LLSGPTAIVT QINHAIGANS EELNVFGLTP EQYILKGEAT QCISGFTAMD ATLLGPLWIL 250 260 GDVFMRPYHT VFDYGNLLVG FAEAA

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. 1 hit. PS50015. SAP_B. Partial match. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CARDH_CYNCA

Accession

Primary (citable) accession number: P85139

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)