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P05805 (CAC3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proproteinase E
Alternative name(s):
Procarboxypeptidase A complex component III
Procarboxypeptidase A-S6 subunit III
Short name=PROCPA-S6 III
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Defective elastase-like serine protease. Does not seem to have a protease activity. Its likely function is to protect procarboxypeptidase a against denaturation in the acidic environment of the ruminant duodenum.

Subunit structure

Monomer. The zymogen is secreted as a ternary complex composed of procarboxypeptidase A, chymotrypsinogen C and proproteinase E.

Subcellular location

Secreted › extracellular space.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Molecular functionSerine protease homolog
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111Activation peptide
PRO_0000028446
Chain12 – 253242Proproteinase E
PRO_0000028447

Regions

Domain12 – 251240Peptidase S1

Amino acid modifications

Disulfide bond41 ↔ 57 Ref.2
Disulfide bond100 ↔ 103 Ref.2
Disulfide bond140 ↔ 206 Ref.2
Disulfide bond171 ↔ 187 Ref.2
Disulfide bond196 ↔ 227 Ref.2

Secondary structure

1 ................................................. 253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05805 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 24663724D8AE409C

FASTA25327,338
        10         20         30         40         50         60 
FSQPFSRPSS RVVNGEDAVP YSWSWQVSLQ YEKDGAFHHT CGGSLIAPDW VVTAGHCIST 

        70         80         90        100        110        120 
SRTYQVVLGE YDRSVLEGSE QVIPINAGDL FVHPLWNSNC VACGNDIALV KLSRSAQLGD 

       130        140        150        160        170        180 
KVQLANLPPA GDILPNEAPC YISGWGRLYT GGPLPDKLQQ ALLPVVDYEH CSQWDWWGIT 

       190        200        210        220        230        240 
VKKTMVCAGG DTRSGCNGDS GGPLNCPAAD GSWQVHGVTS FVSAFGCNTI KKPTVFTRVS 

       250 
AFIDWIDETI ASN

« Hide

References

[1]"Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III."
Pascual R., Vendrell J., Aviles F.X., Bonicel J., Wicker C., Puigserver A.
FEBS Lett. 277:37-41(1990) [PubMed: 2269366] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25.
[2]"Amino acid sequence and disulfide bridges of subunit III, a defective endopeptidase present in the bovine pancreatic 6 S procarboxypeptidase A complex."
Venot N., Sciaky M., Puigserver A., Desnuelle P., Laurent G.
Eur. J. Biochem. 157:91-99(1986) [PubMed: 3519215] [Abstract]
Cited for: PROTEIN SEQUENCE OF 14-253, DISULFIDE BONDS.
[3]"Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E."
Pignol D., Gaboriaud C., Michon T., Kerfelec B., Chapus C., Fontecilla-Camps J.-C.
EMBO J. 13:1763-1771(1994) [PubMed: 8168476] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[4]"The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C."
Gomis-Rueth F.-X., Gomez M., Bode W., Huber R., Aviles F.X.
EMBO J. 14:4387-4394(1995) [PubMed: 7556081] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH CTRC AND PPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

IPIIPI00707244.
PIRCPBOA3. A25065.
UniGeneBt.87229.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FONX-ray1.70A/B14-253[»]
1PYTX-ray2.35C1-253[»]
ProteinModelPortalP05805.
SMRP05805. Positions 6-253.
ModBaseSearch...

Protein-protein interaction databases

STRINGP05805.

Protein family/group databases

MEROPSS01.983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG16139.
HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP05805.

Entry information

Entry nameCAC3_BOVIN
AccessionPrimary (citable) accession number: P05805
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 15, 1998
Last modified: September 21, 2011
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

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