Reviewed, UniProtKB/Swiss-Prot P32951 (CARP1_CANPA)

Names and origin

Protein names

Recommended name:
    Candidapepsin-1
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 1
    ACP 1

Gene names

Name:	SAPP1
Synonyms:	ACPR

Organism

Candida parapsilosis (Yeast)

Taxonomic identifier

5480 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	402 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	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
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 – 62

37

Activation peptide

PRO_0000025869

Chain

63 – 402

340

Candidapepsin-1

PRO_0000025870

Sites

Active site

94

1

By similarity

Active site

282

1

By similarity

Amino acid modifications

Glycosylation

52

1

N-linked (GlcNAc...) Potential

Disulfide bond

109 ↔ 115

By similarity

Disulfide bond

320 ↔ 354

By similarity

Secondary structure

1

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402

Helix Strand Turn

Details...

Beta strand

65 – 67

3

Beta strand

76 – 82

7

Beta strand

87 – 93

7

Beta strand

101 – 108

8

Helix

123 – 125

3

Beta strand

145 – 147

3

Beta strand

168 – 175

8

Helix

185 – 187

3

Helix

205 – 211

7

Beta strand

216 – 222

7

Beta strand

234 – 236

3

Beta strand

249 – 253

5

Beta strand

256 – 258

3

Beta strand

265 – 268

4

Beta strand

272 – 274

3

Helix

292 – 301

10

Beta strand

305 – 310

6

Beta strand

313 – 318

6

Beta strand

328 – 331

4

Beta strand

337 – 340

4

Helix

342 – 345

4

Helix

371 – 373

3

Beta strand

376 – 380

5

Turn

381 – 384

4

Beta strand

385 – 391

7

Sequences

	Sequence		Length	Mass (Da)
	P32951-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 38B06222F52BC1EA	FASTA	402	42,833
	10 20 30 40 50 60 MVAIVTLTRQ VLLTIALALF AQGAAIPEEA AKRDDNPGFV ALDFDVLRKP LNLTEALLRE 70 80 90 100 110 120 KRDSISLSLI NEGPSYASKV SVGSNKQQQT VIIDTGSSDF WVVDSNAQCG KGVDCKSSGT 130 140 150 160 170 180 FTPSSSSSYK NLGAAFTIRY GDGSTSQGTW GKDTVTINGV SITGQQIADV TQTSVDQGIL 190 200 210 220 230 240 GIGYTSNEAV YDTSGRQTTP NYDNVPVTLK KQGKIRTNAY SLYLNSPSAE TGTIIFGGVD 250 260 270 280 290 300 NAKYSGKLVA EQVTSSQPLT ISLASVNLKG SSFSFGDGAL LDSGTTLTYF PSDFAAQLAD 310 320 330 340 350 360 KAGARLVQVA RDQYLYFIDC NTDTSGTTVF NFGNGAKITV PNTEYVYQNG DGTCLWGIQP 370 380 390 400 SDDTILGDNF LRHAYYLLYN LDANTISIAQ VKYTTDSSIS AV

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], PROTEIN SEQUENCE OF 63-77. Strain: Isolate CHUV E18.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z11919 Genomic DNA. Translation: CAA77977.1.

PIR

B47701.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FV3	X-ray	1.85	A/B/C/D/E/F/G/H	63-402	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.4.23.24. 3487.

Family and domain databases

InterPro

IPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[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]

ProtoNet

Search...

Entry information

Entry name

CARP1_CANPA

Accession

Primary (citable) accession number: P32951

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 1, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)