O42779 (CARP9_CANAX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Candidapepsin-9
EC=3.4.23.24

Alternative name(s):
ACP 9
Aspartate protease 9
Secreted aspartic protease 9

Gene names

Name:

SAP9

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	544 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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	Disulfide bond Glycoprotein Zymogen
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 – 17	17	Potential
	Propeptide	18 – ?		Activation peptide Potential		PRO_0000025864
	Chain	? – 544		Candidapepsin-9		PRO_0000025865
Sites
	Active site	167	1	By similarity
	Active site	371	1	By similarity
Amino acid modifications
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	240	1	N-linked (GlcNAc...) Potential
	Glycosylation	252	1	N-linked (GlcNAc...) Potential
	Glycosylation	422	1	N-linked (GlcNAc...) Potential
	Glycosylation	499	1	N-linked (GlcNAc...) Potential
	Disulfide bond	406 ↔ 441		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O42779 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E6D755A46040A486	FASTA	544	58,625
	10 20 30 40 50 60 MRLNSVALLS LVATALAAKA PFKIDFEVRR GESKDDLSPE DDSNPRFVKR DGSLDMTLTN 70 80 90 100 110 120 KQTFYMATLK IGSNEDENRV LEDTGSSDLW VMSHDLKCVS APISKRNERS FGHGTGVKLN 130 140 150 160 170 180 ERELMQKRKN LYQPSRTIET DEEKEASEKI HNKLFGFGSI YSTVYITEGP GAYSTFSPLV 190 200 210 220 230 240 GTEGGSGGSG GSNTCRSYGS FNTENSDTFK KNNTNDFEIQ YADDTSAIGI WGYDDVTISN 250 260 270 280 290 300 VTVKDLSFAI ANETSSDVGV LGIGLPGLEV TTQLRYTYQN LPLKLKADGI IAKSLYSLYL 310 320 330 340 350 360 NTADAKAGSI LFGAIDHAKY QGDLVTVKMM RTYSQISYPV RIQVPVLKID VESSSGSTTN 370 380 390 400 410 420 ILSGTTGVVL DTGSTLSYVF SDTLQSLGKA LNGQYSNSVG AYVVNCNLAD SSRTVDIEFG 430 440 450 460 470 480 GNKTIKVPIS DLVLQASKST CILGVMQQSS SSSYMLFGDN ILRSAYIVYD LDDYEVSLAQ 490 500 510 520 530 540 VSYTNKESIE VIGASGITNS SGSGTTSSSG TSTSTSTRHS AGSIISNPVY GLLLSLLISY YVLV

References

[1]	"Differential regulation of SAP8 and SAP9, which encode two new members of the secreted aspartic proteinase family in Candida albicans." Monod M., Hube B., Hess D., Sanglard D. Microbiology 144:2731-2737(1998) [PubMed: 9802014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C74.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF043331 Genomic DNA. Translation: AAC69996.1.
3D structure databases
ProteinModelPortal	O42779.
ModBase	Search...
Protein family/group databases
MEROPS	A01.067.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 3 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 2 hits. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARP9_CANAX

Accession

Primary (citable) accession number: O42779

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 1, 1998
Last modified:	November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program