C4YMJ3 (CARP2_CANAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Candidapepsin-2
EC=3.4.23.24

Alternative name(s):
ACP 2
Aspartate protease 2
Secreted aspartic protease 2

Gene names

Name:	SAP2
Synonyms:	PRA11, PRA2
ORF Names:	CAWG_02075

Organism

Candida albicans (strain WO-1) (Yeast) [Complete proteome]

Taxonomic identifier

294748 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida › Candida albicans

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted.
Post-translational modification	O-glycosylated By similarity.
Miscellaneous	Expressed both in W (white) and in O (opaque) cells of strain WO-1.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 56	38	Activation peptide		PRO_0000413050
	Chain	57 – 398	342	Candidapepsin-2		PRO_0000413051
Regions
	Region	88 – 90	3	Inhibitor binding By similarity
	Region	141 – 142	2	Inhibitor binding By similarity
	Region	274 – 278	5	Inhibitor binding By similarity
Sites
	Active site	88	1	By similarity
	Active site	274	1	By similarity
Amino acid modifications
	Glycosylation	313	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Disulfide bond	103 ↔ 115		By similarity
	Disulfide bond	312 ↔ 350		By similarity

Sequences

	Sequence		Length	Mass (Da)
	C4YMJ3 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 76D3516B8B9BA8F4	FASTA	398	42,315
	10 20 30 40 50 60 MFLKNIFIGL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE GKTSKRQAVP 70 80 90 100 110 120 VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN VDCQVTYSDQ TADFCKQKGT 130 140 150 160 170 180 YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL YKDTVGFGGV SIKNQVLADV DSTSIDQGIL 190 200 210 220 230 240 GVGYKTNEAG GSYDNVPVTL KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI 250 260 270 280 290 300 ALPVTSDREL RISLGSVEVS GKTINTDNVD VLLDSGTTIT YLQQDLADQI IKAFNGKLTQ 310 320 330 340 350 360 DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC QLLFDVNDAN 370 380 390 ILGDNFLRSA YIVYDLDNNE ISLAQVKYTS ASSISALT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: WO-1.
[2]	"Three distinct secreted aspartyl proteinases in Candida albicans." White T.C., Miyasaki S.H., Agabian N. J. Bacteriol. 175:6126-6133(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-71. Strain: WO-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000309 Genomic DNA. Translation: EEQ43824.1.
3D structure databases
ModBase	Search...
Protein family/group databases
Allergome	1436. Cand a CAAP.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HOG000248646.
OMA	CANGACE.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARP2_CANAW

Accession

Primary (citable) accession number: C4YMJ3
Secondary accession number(s): P28871, P43097

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	July 28, 2009
Last modified:	April 3, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program