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P06026 (CARP_RHICH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. 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:
Rhizopuspepsin

EC=3.4.23.21
OrganismRhizopus chinensis (Bread mold)
Taxonomic identifier4843 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   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

Signal peptide1 – 2121 Potential
Propeptide22 – 6847Activation peptide Probable
PRO_0000025881
Chain69 – 393325Rhizopuspepsin
PRO_0000025882

Sites

Active site1031 By similarity
Active site2861 By similarity

Amino acid modifications

Disulfide bond116 ↔ 119
Disulfide bond320 ↔ 353

Natural variations

Natural variant831V → I.
Natural variant1291K → N.
Natural variant1841N → S.
Natural variant2301S → K.
Natural variant2981V → I.
Natural variant3091S → Y.
Natural variant3611N → D.
Natural variant3931Q → E.

Secondary structure

..................................................................... 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06026 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 479BBDB3D001D25C

FASTA39341,327
        10         20         30         40         50         60 
MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI AKYNKHKINT 

        70         80         90        100        110        120 
STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL DFDTGSSDLW IASTLCTNCG 

       130        140        150        160        170        180 
SRQTKYDPKQ SSTYQADGRT WSISYGDGSS ASGILAKDNV NLGGLLIKGQ TIELAKREAA 

       190        200        210        220        230        240 
SFANGPNDGL LGLGFDTITT VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG 

       250        260        270        280        290        300 
GYDSTKFKGS LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA 

       310        320        330        340        350        360 
SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ GQCIAGFGYG 

       370        380        390 
NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ 

« Hide

References

[1]Gregoli P.A., Delaney R.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Amino acid sequence of rhizopuspepsin isozyme pI 5."
Delaney R., Wong R.N.S., Meng G.-Z., Wu N.-H., Tang J.
J. Biol. Chem. 262:1461-1467(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-393.
[3]"The amino acid sequence of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis."
Takahashi K.
J. Biol. Chem. 262:1468-1478(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-393.
[4]"Homology among acid proteases: comparison of crystal structures at 3-A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica."
Subramanian E., Swan I.D.A., Liu M., Davies D.R., Jenkins J.A., Tickle I.J., Blundell T.L.
Proc. Natl. Acad. Sci. U.S.A. 74:556-559(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-392.
[5]"Structure and refinement at 1.8-A resolution of the aspartic proteinase from Rhizopus chinensis."
Suguna K., Bott R.R., Padlan E.A., Subramanian E., Sheriff S., Cohen G.H., Davies D.R.
J. Mol. Biol. 196:877-900(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 69-392.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33859 Genomic DNA. Translation: AAB59306.1.
L33858 Genomic DNA. Translation: AAB59305.1.
J02651 mRNA. Translation: AAA33879.1.
PIRA26681.
A41415.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UH7X-ray2.10A69-392[»]
1UH8X-ray2.30A69-392[»]
1UH9X-ray2.00A69-392[»]
2APRX-ray1.80A69-392[»]
3APRX-ray1.80E69-392[»]
4APRX-ray2.50E69-392[»]
5APRX-ray2.10E69-392[»]
6APRX-ray2.50E69-392[»]
ProteinModelPortalP06026.
SMRP06026. Positions 69-393.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP06026.
ChEMBLCHEMBL4253.

Protein family/group databases

MEROPSA01.012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06026.

Entry information

Entry nameCARP_RHICH
AccessionPrimary (citable) accession number: P06026
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1996
Last modified: December 11, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references