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Reviewed, UniProtKB/Swiss-Prot P10977 (CARPV_CANAL)

Last modified November 24, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Vacuolar aspartic protease
    EC=3.4.23.-
Alternative name(s):
    Aspartate protease
    ACP
Gene names
Name: APR1
Synonyms: PRA, PRA1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Subcellular location

Vacuole. Note: Lysosome-like vacuoles Potential.

Sequence similarities

Belongs to the peptidase A1 family.

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Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 419397Vacuolar aspartic protease
PRO_0000025866

Regions

Motif417 – 4193Microbody targeting signal Potential

Sites

Active site1221 By similarity
Active site3071 By similarity

Amino acid modifications

Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Disulfide bond135 ↔ 140 By similarity
Disulfide bond341 ↔ 374 By similarity

Experimental info

Sequence conflict39 – 402DA → MH in CAA31962. Ref.2
Sequence conflict881K → E in CAA31962. Ref.2
Sequence conflict1091Q → E in CAA31962. Ref.2
Sequence conflict1561V → A in CAA31962. Ref.2
Sequence conflict174 – 1752IS → HI in CAA31962. Ref.2
Sequence conflict2341G → A in CAA31962. Ref.2
Sequence conflict2811A → D in CAA31962. Ref.2
Sequence conflict367 – 3682IL → Y in CAA31962. Ref.2
Sequence conflict4171T → S in CAA31962. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P10977-1 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: C283B2968EAED887

FASTA41945,421
        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

« Hide

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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 / IFO 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 / IFO 1393.

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Cross-references

Sequence databases

U36754 Genomic DNA. Translation: AAA79879.1.
X13669 Genomic DNA. Translation: CAA31962.1.
PIRS03433.

3D structure databases

SMRP10977. Positions 90-415.
ModBaseSearch...

Protein family/group databases

MEROPSA01.018.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCARPV_CANAL
AccessionPrimary (citable) accession number: P10977
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: November 24, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents