P10977 (CARPV_CANAX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar aspartic protease
EC=3.4.23.-

Alternative name(s):
ACP
Aspartate protease

Gene names

Name:	APR1
Synonyms:	PRA, PRA1

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Subcellular location	Vacuole. Note: Lysosome-like vacuoles Potential.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	vacuole 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 – 22	22	Potential
	Chain	23 – 419	397	Vacuolar aspartic protease		PRO_0000025866
Regions
	Motif	417 – 419	3	Microbody targeting signal Potential
Sites
	Active site	122	1	By similarity
	Active site	307	1	By similarity
Amino acid modifications
	Glycosylation	157	1	N-linked (GlcNAc...) Potential
	Glycosylation	358	1	N-linked (GlcNAc...) Potential
	Disulfide bond	135 ↔ 140		By similarity
	Disulfide bond	341 ↔ 374		By similarity
Experimental info
	Sequence conflict	39 – 40	2	DA → MH in CAA31962. Ref.2
	Sequence conflict	88	1	K → E in CAA31962. Ref.2
	Sequence conflict	109	1	Q → E in CAA31962. Ref.2
	Sequence conflict	156	1	V → A in CAA31962. Ref.2
	Sequence conflict	174 – 175	2	IS → HI in CAA31962. Ref.2
	Sequence conflict	234	1	G → A in CAA31962. Ref.2
	Sequence conflict	281	1	A → D in CAA31962. Ref.2
	Sequence conflict	367 – 368	2	IL → Y in CAA31962. Ref.2
	Sequence conflict	417	1	T → S in CAA31962. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10977 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: C283B2968EAED887	FASTA	419	45,421
	10 20 30 40 50 60 MQLSLSALTT VALALTSSLV DAKAHSIKLS KLSNEETLDA SNFQEYTNSL ANKYLNLFNT 70 80 90 100 110 120 AHGNPSNFGL QHVLTNQEAE VPFVTPKKGG KYDAPLTNYL NAQYFTEIQI GTPGQPFKVI 130 140 150 160 170 180 LDTGSSNLWV PSQDCTSLAC FLHAKYDHDA SSTYKVNGSE FSIQYGSGSM EGYISQDVLT 190 200 210 220 230 240 IGDLVIPGQD FAEATSEPGL AFAFGKFDGI LGLAYDTISV NHIVPPIYNA INQGLLEKPQ 250 260 270 280 290 300 FGFYLGSTDK DENDGGLATF GGYDASLFQG KITWLPIRRK AYWEVSFEGI GLGDEYAELH 310 320 330 340 350 360 KTGAAIDTGT SLITLPSSLA EIINAKIGAT KSWSGQYQVD CAKRDSLPDL TLTFAGYNFT 370 380 390 400 410 LTPYDYILEV SGSCISVFTP MDFPQPIGDL AIVGDAFLRK YYSIYDLDKN AVGLAPTKV

References

[1]	"Temperature-related expression of the vacuolar aspartic proteinase (APR1) gene and beta-N-acetylglucosaminidase (HEX1) gene during Candida albicans morphogenesis." Niimi M., Niimi K., Cannon R.D. FEMS Microbiol. Lett. 148:247-254(1997) [PubMed: 9084153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10261 / CBS 2718 / NBRC 1061.
[2]	"Nucleotide sequence of the Candida albicans aspartyl proteinase gene." Lott T.J., Boiron P., Page L.S., Benson J., Reiss E. Nucleic Acids Res. 17:1779-1779(1989) [PubMed: 2646602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-419. Strain: ATCC 2091 / CBS 2730 / DSM 1665 / CIP 1180.79 / NBRC 1393.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36754 Genomic DNA. Translation: AAA79879.1. X13669 Genomic DNA. Translation: CAA31962.1.
PIR	S03433.
3D structure databases
ProteinModelPortal	P10977.
SMR	P10977. Positions 90-415.
ModBase	Search...
Protein-protein interaction databases
STRING	P10977.
Protein family/group databases
MEROPS	A01.018.
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. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 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...

Entry information

Entry name

CARPV_CANAX

Accession

Primary (citable) accession number: P10977

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program