Reviewed, UniProtKB/Swiss-Prot P28872 (CARP1_CANAL)

Names and origin

Protein names

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

Gene names

Name:	SAP1
Synonyms:	PRA10, PRA3

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	391 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.
Miscellaneous	Expressed exclusively in O (opaque) cells and not in W (white) cells of strain WO-1.
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 Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 50	32	Activation peptide By similarity
	Chain	51 – 391	341	Candidapepsin-1
Sites
	Active site	82	1	By similarity
	Active site	267	1	By similarity
Amino acid modifications
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
	Disulfide bond	97 ↔ 109		By similarity
	Disulfide bond	305 ↔ 343		By similarity
Natural variations
	Natural variant	53	1	I → L in allele 2.4 and allele 2.6.
	Natural variant	131	1	Y → N in allele 2.6.
	Natural variant	319	1	A → V in allele 2.6.
Experimental info
	Sequence conflict	61	1	H → L in CAA40192. Ref.1
	Sequence conflict	128	1	T → S in CAA40192. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P28872-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: CF88C56943BCCCA9	FASTA	391	41,602
	10 20 30 40 50 60 MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QAIPVTLNNE 70 80 90 100 110 120 HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS 130 140 150 160 170 180 TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT 190 200 210 220 230 240 NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS 250 260 270 280 290 300 DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF 310 320 330 340 350 360 YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL 370 380 390 RSAYLVYDLD DDKISLAQVK YTSASNIAAL T

References

[1]	"Sequence of the Candida albicans gene encoding the secretory aspartate proteinase." Hube B., Turver C.J., Odds F.C., Eiffert H., Boulnois G.J., Koechel H., Ruechel R. J. Med. Vet. Mycol. 29:129-132(1991) [PubMed: 1880680] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 10231 / CBS 6431 / DSM 1386 / IFO 1594.
[2]	"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: 7907585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SS and WO-1.
[3]	"The 'universal' leucine codon CTG in the secreted aspartyl proteinase 1 (SAP1) gene of Candida albicans encodes a serine in vivo." White T.C., Andrews L.E., Maltby D., Agabian N. J. Bacteriol. 177:2953-2955(1995) [PubMed: 7751316] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[4]	"Three distinct secreted aspartyl proteinases in Candida albicans." White T.C., Miyasaki S.H., Agabian N. J. Bacteriol. 175:6126-6133(1993) [PubMed: 8407785] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-65. Strain: WO-1.
[5]	"Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes." Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F. Microbiology 143:349-356(1997) [PubMed: 9043112] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56867 Genomic DNA. Translation: CAA40192.1. L12449 Genomic DNA. Translation: AAA34368.2. L12450 Genomic DNA. Translation: AAA34369.2. L12451 Genomic DNA. Translation: AAA34370.2. L12452 Genomic DNA. Translation: AAA34371.2.
3D structure databases
HSSP	HSSP built from PDB template 1EAG based on UniProtKB P28871.
SMR	P28872. Positions 51-391.
ModBase	Search...
Protein family/group databases
MEROPS	A01.014.
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. [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]
ProDom	P28872. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CARP1_CANAL

Accession

Primary (citable) accession number: P28872

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	November 1, 1995
Last modified:	July 22, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)