Reviewed, UniProtKB/Swiss-Prot P43096 (CARP7_CANAL)

Names and origin

Protein names

Recommended name:
    Candidapepsin-7
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 7
    ACP 7
    Secreted aspartic protease 7

Gene names

Name:

SAP7

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	588 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
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 – 16	16	Potential
	Propeptide	17 – 211	195	Activation peptide Potential		PRO_0000025860
	Chain	212 – 588	377	Candidapepsin-7		PRO_0000025861
Regions
	Compositional bias	180 – 190	11	Poly-Ser
Sites
	Active site	244	1	By similarity
	Active site	464	1	By similarity
Amino acid modifications
	Glycosylation	150	1	N-linked (GlcNAc...) Potential
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Glycosylation	308	1	N-linked (GlcNAc...) Potential
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
	Glycosylation	423	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	486	1	N-linked (GlcNAc...) Potential
	Disulfide bond	260 ↔ 269		By similarity
	Disulfide bond	500 ↔ 540		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43096-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 01C676FC39C21D61	FASTA	588	62,553
	10 20 30 40 50 60 MQRVLELLLL SSTALAVIGD GFIALPVHKL QAGEGSAHFP NRLPIFDVVN GVAKSVEDDV 70 80 90 100 110 120 NQIIQPIFGN GIFSGGSIQG THSGNGHSVK YEVSLPSSSA QKGSNGPSST DNKDTDPSKT 130 140 150 160 170 180 GFSLDDLMNS ISTDFWNLIG LNKPPTSSDN GSKDADFTPS AVSQVEQPTS KSVESTAPGS 190 200 210 220 230 240 ASSASSSSSS EAASSSQPSE DSQPSSSANK KTGAFFLSLD NTQTLYTATL KVGSPAQEVQ 250 260 270 280 290 300 VMIDTGSSDL WFISSGNSQC KVNGGSIDCD KYGVFDKSKS SSWHDNKTDY SISYYDGDKA 310 320 330 340 350 360 SGTMGQDNIT FADGFSIENA NFAVIDNTTS SIGVFGVGYP ELEAVKSKYT NLPFAMKEQN 370 380 390 400 410 420 LIAKVAYSLY LDSRDAVQGY ILFGGIDHAF YTGDLKAFDI VQCNDKYVYS QIPLTSVASS 430 440 450 460 470 480 LNNYTNAYGL PAGSNHPKVG AVIYNGTDSF NGGVDLKDTL TLLDTGTTYS YLSKDQVESI 490 500 510 520 530 540 VGLYGNVTYN DAGKAYEVPC WVGNPGNYLE FNFKNEQYIK VPTSEFVISV GTYASGAELC 550 560 570 580 VFGILPGTHS ILGDNFMRSV YAVFDLEDHV ISIAQAAYND NHAVVPIE

References

[1]	"Multiplicity of genes encoding secreted aspartic proteinases in Candida species." Monod M., Togni G., Hube B., Sanglard D. Mol. Microbiol. 13:357-368(1994) [PubMed: 7984113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C74.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z30193 Genomic DNA. Translation: CAA82925.1.
PIR	S42074. S49058.
3D structure databases
HSSP	HSSP built from PDB template 1ZAP based on UniProtKB P28871.
ModBase	Search...
Protein family/group databases
MEROPS	A01.065.
Enzyme and pathway databases
BRENDA	3.4.23.24. 1124.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. [Graphical view]
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARP7_CANAL

Accession

Primary (citable) accession number: P43096

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)