P43094 (CARP5_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Candidapepsin-5
EC=3.4.23.24

Alternative name(s):
ACP 5
Aspartate protease 5
Secreted aspartic protease 5

Gene names

Name:	SAP5
ORF Names:	CaO19.5585, CaO19.13032

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	418 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.
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	3D-structure
Gene Ontology (GO)
Biological process	pathogenesis Inferred from mutant phenotype. Source: CGD proteolysis Inferred from direct assay. Source: CGD
Cellular component	extracellular region Inferred from direct assay. Source: CGD intracellular Inferred from direct assay. Source: CGD
Molecular function	aspartic-type endopeptidase activity Inferred from direct assay. Source: CGD
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 – 76

58

Activation peptide Potential

PRO_0000025856

Chain

77 – 418

342

Candidapepsin-5

PRO_0000025857

Sites

Active site

108

1

By similarity

Active site

294

1

By similarity

Amino acid modifications

Disulfide bond

123 ↔ 135

By similarity

Disulfide bond

332 ↔ 370

By similarity

Secondary structure

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418

Helix Strand Turn

Details...

Beta strand

79 – 81

3

Beta strand

90 – 96

7

Beta strand

101 – 107

7

Beta strand

115 – 123

9

Helix

134 – 136

3

Helix

143 – 145

3

Beta strand

165 – 167

3

Beta strand

169 – 175

7

Beta strand

182 – 193

12

Beta strand

210 – 212

3

Helix

217 – 223

7

Beta strand

231 – 234

4

Beta strand

246 – 248

3

Beta strand

261 – 264

4

Beta strand

268 – 270

3

Beta strand

277 – 280

4

Beta strand

284 – 286

3

Beta strand

291 – 293

3

Beta strand

299 – 302

4

Helix

304 – 313

10

Beta strand

317 – 320

4

Beta strand

326 – 330

5

Beta strand

338 – 342

5

Beta strand

346 – 350

5

Helix

352 – 355

4

Beta strand

368 – 376

9

Helix

387 – 389

3

Beta strand

390 – 395

6

Turn

396 – 399

4

Beta strand

400 – 406

7

Sequences

	Sequence		Length	Mass (Da)
	P43094 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 185B00E6BA4AD1E6	FASTA	418	45,649
	10 20 30 40 50 60 MFLKNILSVL AFALLIDAAP VKRSPGFVTL DFNVKRSLVD PDDPTVEAKR SPLFLEFTPS 70 80 90 100 110 120 EFPVDETGRD GDVDKRGPVA VTLHNEAITY TADITVGSDN QKLNVIVDTG SSDLWIPDSN 130 140 150 160 170 180 VICIPKWRGD KGDFCKSAGS YSPASSRTSQ NLNTRFDIKY GDGSYAKGKL YKDTVGIGGV 190 200 210 220 230 240 SVRDQLFANV WSTSARKGIL GIGFQSGEAT EFDYDNLPIS LRNQGIIGKA AYSLYLNSAE 250 260 270 280 290 300 ASTGQIIFGG IDKAKYSGSL VDLPITSEKK LTVGLRSVNV RGRNVDANTN VLLDSGTTIS 310 320 330 340 350 360 YFTRSIVRNI LYAIGAQMKF DSAGNKVYVA DCKTSGTIDF QFGNNLKISV PVSEFLFQTY 370 380 390 400 410 YTSGKPFPKC EVRIRESEDN ILGDNFLRSA YVVYNLDDKK ISMAPVKYTS ESDIVAIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiplicity of genes encoding secreted aspartic proteinases in Candida species." Monod M., Togni G., Hube B., Sanglard D. Mol. Microbiol. 13:357-368(1994) [PubMed: 7984113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C74.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z30191 Genomic DNA. Translation: CAA82923.1.
AACQ01000034 Genomic DNA. Translation: EAL00252.1.
AACQ01000033 Genomic DNA. Translation: EAL00375.1.

PIR

S42072. S49056.

RefSeq

XP_719147.1. XM_714054.1.
XP_719265.1. XM_714172.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QZX	X-ray	2.50	A/B	77-418	[»]

ProteinModelPortal

P43094.

SMR

P43094. Positions 77-418.

ModBase

Search...

Protein family/group databases

MEROPS

A01.063.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3639155.
3639268.

KEGG

cal:CaO19.13032.
cal:CaO19.5585.

Organism-specific databases

CGD

CAL0006261. SAP5.

Phylogenomic databases

PhylomeDB

P43094.

Enzyme and pathway databases

BRENDA

3.4.23.24. 1096.

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.

KO

K06005.

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...

Other

PMAP-CutDB

P43094.

Entry information

Entry name

CARP5_CANAL

Accession

Primary (citable) accession number: P43094
Secondary accession number(s): Q5ABW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program