P32950 (CARP2_CANPA) 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

Gene names

Name:	SAPP2
Synonyms:	ACPL

Organism

Candida parapsilosis (Yeast)

Taxonomic identifier

5480 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	412 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.
Subcellular location	Secreted.
Post-translational modification	O-glycosylated Probable.
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	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 – 25	25	Or 18, or 21 Potential
	Propeptide	26 – 61	36	Activation peptide		PRO_0000025871
	Chain	62 – 412	351	Candidapepsin-2		PRO_0000025872
Sites
	Active site	93	1	By similarity
	Active site	273	1	By similarity
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Disulfide bond	108 ↔ 113		By similarity
	Disulfide bond	311 ↔ 345		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P32950 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 6D4DE8B954ADC8B3	FASTA	412	44,443
	10 20 30 40 50 60 MTTIAIFTKN VLLAIAFALF AQGAAIPDPA KRDDNPGFVA LDFEVTRKPL DVNATSELSK 70 80 90 100 110 120 RSSPSSPLYF EGPSYGIRVS VGSNKQEQQV VLDTGSSDFW VVDSSASCQK GNCKQYGTFD 130 140 150 160 170 180 PHSSTSFKSL GSSFRSIGYG DKSSSIGTWG QDTIYLGGTS ITNQRFADVT STSVNQGILG 190 200 210 220 230 240 VGRVETESAN PPYDNVPITL KKQGKIKTNA YSLYLNSPGA ATGTIIFGGV DNAKYSGKLI 250 260 270 280 290 300 EEPLVSDRYL AVNLKSLNYN GDNSNAGFGV VVDSGTTISY LPDSIVNDLA NKVGAYLEPV 310 320 330 340 350 360 GLGNELYFID CNANPQGSAS FTFDNGAKIT VPLSEFVLQS TANACVWGLQ SSDRQNVPPI 370 380 390 400 410 LGDNFLRHAY AFQLDKETVL SRSGEVHFCL KCFSNLETSI VWKAFFYNRY IQ

References

[1]	"Cloning and sequencing of two Candida parapsilosis genes encoding acid proteases." de Viragh P.A., Sanglard D., Togni G., Falchetto R., Monod M. J. Gen. Microbiol. 139:335-342(1993) [PubMed: 8436951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate CHUV E18.
[2]	"Candida parapsilosis expresses and secretes two aspartic proteinases." Fusek M., Smith E.A., Monod M., Foundling S.I. FEBS Lett. 327:108-112(1993) [PubMed: 8335087] [Abstract] Cited for: PROTEIN SEQUENCE OF 62-68. Strain: Isolate CHUV E18.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11918 Genomic DNA. Translation: CAA77976.1.
3D structure databases
ProteinModelPortal	P32950.
ModBase	Search...
Protein family/group databases
MEROPS	A01.076.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.4.23.24. 1133.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 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_CANPA

Accession

Primary (citable) accession number: P32950

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program