P32951 (CARP1_CANPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Candidapepsin-1
EC=3.4.23.24

Alternative name(s):
ACP 1
Aspartate protease 1

Gene names

Name:	SAPP1
Synonyms:	ACPR

Organism

Candida parapsilosis (Yeast)

Taxonomic identifier

5480 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › 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: 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 – 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 – 71

7

Beta strand

73 – 82

10

Turn

83 – 86

4

Beta strand

87 – 94

8

Beta strand

100 – 109

10

Turn

115 – 118

4

Helix

123 – 125

3

Beta strand

130 – 139

10

Beta strand

145 – 157

13

Beta strand

160 – 177

18

Beta strand

179 – 181

3

Helix

185 – 187

3

Helix

205 – 211

7

Beta strand

216 – 223

8

Beta strand

230 – 236

7

Beta strand

238 – 240

3

Beta strand

243 – 246

4

Beta strand

249 – 253

5

Beta strand

256 – 258

3

Beta strand

260 – 270

11

Beta strand

272 – 281

10

Beta strand

286 – 290

5

Helix

292 – 302

11

Beta strand

305 – 310

6

Beta strand

313 – 318

6

Beta strand

326 – 332

7

Beta strand

337 – 341

5

Helix

342 – 345

4

Beta strand

346 – 348

3

Beta strand

350 – 352

3

Beta strand

354 – 360

7

Helix

368 – 371

4

Beta strand

376 – 380

5

Turn

381 – 384

4

Beta strand

385 – 391

7

Beta strand

399 – 401

3

Sequences

	Sequence		Length	Mass (Da)
	P32951 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 63-77. Strain: Isolate CHUV E18.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z11919 Genomic DNA. Translation: CAA77977.1.

PIR

B47701.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FV3	X-ray	1.85	A/B/C/D/E/F/G/H	63-402	[»]
3TNE	X-ray	2.40	A/B	63-402	[»]

ProteinModelPortal

P32951.

ModBase

Search...

Protein family/group databases

MEROPS

A01.038.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.23.24. 1133.

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...

Other

EvolutionaryTrace

P32951.

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:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program