P43093 (CARP4_CANAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Candidapepsin-4
EC=3.4.23.24

Alternative name(s):
ACP 4
Aspartate protease 4
Secreted aspartic protease 4

Gene names

Name:	SAP4
ORF Names:	CAWG_05020

Organism

Candida albicans (strain WO-1) (Yeast) [Complete proteome]

Taxonomic identifier

294748 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida › Candida albicans

Protein attributes

Sequence length	417 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	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
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 – 18	18	Potential
	Propeptide	19 – 75	57	Activation peptide		PRO_0000025854
	Chain	76 – 417	342	Candidapepsin-4		PRO_0000025855
Sites
	Active site	107	1	By similarity
	Active site	293	1	By similarity
Amino acid modifications
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Disulfide bond	122 ↔ 134		By similarity
	Disulfide bond	331 ↔ 369		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43093 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 79634304469FB60A	FASTA	417	45,318
	10 20 30 40 50 60 MFLQNILSVL AFALLIDAAP VKRSTGFVTL DFNVKRSLVD PKDPTVEVKR SPLFLDIEPT 70 80 90 100 110 120 EIPVDDTGRN DVGKRGPVAV KLDNEIITYS ADITIGSNNQ KLSVIVDTGS SDLWVPDSNA 130 140 150 160 170 180 VCIPKWPGDR GDFCKNNGSY SPAASSTSKN LNTPFEIKYA DGSVAQGNLY QDTVGIGGVS 190 200 210 220 230 240 VRDQLFANVR STSAHKGILG IGFQSNEATR TPYDNLPITL KKQGIISKNA YSLFLNSPEA 250 260 270 280 290 300 SSGQIIFGGI DKAKYSGSLV DLPITSDRTL SVGLRSVNVM GQNVNVNAGV LLDSGTTISY 310 320 330 340 350 360 FTPNIARSII YALGGQVHYD SSGNEAYVAD CKTSGTVDFQ FDRNLKISVP ASEFLYQLYY 370 380 390 400 410 TNGEPYPKCE IRVRESEDNI LGDNFMRSAY IVYDLDDRKI SMAQVKYTSQ SNIVGIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive element are located upstream of the SAP1 gene in Candida albicans." Miyasaki S.H., White T.C., Agabian N. J. Bacteriol. 176:1702-1710(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WO-1.
[2]	"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: WO-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L25388 Unassigned DNA. Translation: AAA17877.1. CM000312 Genomic DNA. Translation: EEQ46658.1.
PIR	A55524.
3D structure databases
ProteinModelPortal	P43093.
SMR	P43093. Positions 76-417.
ModBase	Search...
Protein family/group databases
MEROPS	A01.062.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG248628.
HOGENOM	HOG000248646.
OMA	PNIARSI.
Enzyme and pathway databases
BRENDA	3.4.23.24. 1096.
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
ChEMBL	CHEMBL6179.
PMAP-CutDB	P43093.

Entry information

Entry name

CARP4_CANAW

Accession

Primary (citable) accession number: P43093
Secondary accession number(s): C4YSF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program