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P17576 (CARP_IRPLA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyporopepsin

EC=3.4.23.29
Alternative name(s):
Aspartic proteinase
OrganismIrpex lacteus (Milk-white toothed polypore) (Polyporus tulipiferae)
Taxonomic identifier5319 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPolyporales incertae sedisIrpex

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Milk clotting activity, broad specificity, but fails to cleave 15-Leu-|-Tyr-16 or 16-Tyr-|-Leu-17 of insulin B chain.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Polyporopepsin
PRO_0000199512

Sites

Active site321
Active site2121

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential

Secondary structure

................................................................... 340
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17576 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 9BAF837264D42FEF

FASTA34035,051
        10         20         30         40         50         60 
AAGSVPATNQ LVDYVVNVGV GSPATTYSLL VDTGSSNTWL GADKSYVKTS TSSATSDKVS 

        70         80         90        100        110        120 
VTYGSGSFSG TEYTDTVTLG SLTIPKQSIG VASRDSGFDG VDGILGVGPV DLTVGTLSPH 

       130        140        150        160        170        180 
TSTSIPTVTD NLFSQGTIPT NLLAVSFEPT TSESSTNGEL TFGATDSSKY TGSITYTPIT 

       190        200        210        220        230        240 
STSPASAYWG INQTIRYGSS TSILSSTAGI VDTGTTLTLI ASDAFAKYKK ATGAVADNNT 

       250        260        270        280        290        300 
GLLRLTTAQY ANLQSLFFTI GGQTFELTAN AQIWPRNLNT AIGGSASSVY LIVGDLGSDS 

       310        320        330        340 
GEGLDFINGL TFLERFYSVY DTTNKRLGLA TTSFTTATSN 

« Hide

References

[1]"Cloning and sequence analysis of cDNA for Irpex lacteus aspartic proteinase."
Kobayashi H., Sekibata S., Shibuya H., Yoshida S., Kusakabe I., Murakami K.
Agric. Biol. Chem. 53:1927-1933(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-24.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00589 mRNA. Translation: BAA00467.1.
PIRPEIKL. JU0057.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WKRX-ray1.30A1-340[»]
ProteinModelPortalP17576.
SMRP17576. Positions 1-340.
ModBaseSearch...

Protein family/group databases

MEROPSA01.019.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17576.

Entry information

Entry nameCARP_IRPLA
AccessionPrimary (citable) accession number: P17576
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: March 6, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families