Reviewed, UniProtKB/Swiss-Prot P43092 (CARP3_CANAL)

Names and origin

Protein names

Recommended name:
    Candidapepsin-3
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 3
    ACP 3
    Secreted aspartic protease 3

Gene names

Name:

SAP3

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

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.
Subcellular location	Secreted.
Post-translational modification	O-glycosylated By similarity.
Miscellaneous	Expressed exclusively in O (opaque) cells and not in W (white) 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 Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 58	40	Activation peptide
	Chain	59 – 398	340	Candidapepsin-3
Sites
	Active site	90	1	By similarity
	Active site	274	1	By similarity
Amino acid modifications
	Glycosylation	42	1	N-linked (GlcNAc...) Potential
	Glycosylation	313	1	N-linked (GlcNAc...) Potential
	Disulfide bond	105 ↔ 116		By similarity
	Disulfide bond	312 ↔ 350		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43092-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D9A8687FBAD4C448	FASTA	398	42,806
	10 20 30 40 50 60 MFLKNIFIAL AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT 70 80 90 100 110 120 VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG 130 140 150 160 170 180 TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI 190 200 210 220 230 240 LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL 250 260 270 280 290 300 IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY 310 320 330 340 350 360 DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN 370 380 390 ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT

References

[1]	"Three distinct secreted aspartyl proteinases in Candida albicans." White T.C., Miyasaki S.H., Agabian N. J. Bacteriol. 175:6126-6133(1993) [PubMed: 8407785] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 59-73. Strain: SS.
[2]	"Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes." Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F. Microbiology 143:349-356(1997) [PubMed: 9043112] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L22358 Genomic DNA. Translation: AAA34372.1.

PIR

A36926.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H6S	X-ray	2.20	A	59-398	[»]
2H6T	X-ray	1.90	A	59-398	[»]

ModBase

Search...

Protein family/group databases

MEROPS

A01.061.

Organism-specific databases

CGD

CAL0005017. SAP3.

Family and domain databases

InterPro

IPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
[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. 2 hits.
[Graphical view]

ProDom

P43092.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

ProtoNet

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Entry information

Entry name

CARP3_CANAL

Accession

Primary (citable) accession number: P43092

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	July 22, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)