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P00767 (CTRB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsinogen B

EC=3.4.21.1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Chain1 – 1313Chymotrypsin B chain A
PRO_0000027629
Propeptide14 – 152
PRO_0000027630
Chain16 – 146131Chymotrypsin B chain B
PRO_0000027631
Propeptide147 – 1482
PRO_0000027632
Chain149 – 24597Chymotrypsin B chain C
PRO_0000027633

Regions

Domain16 – 243228Peptidase S1

Sites

Active site571Charge relay system Ref.1
Active site1021Charge relay system Ref.1
Active site1951Charge relay system Ref.1

Amino acid modifications

Disulfide bond1 ↔ 122 Ref.1
Disulfide bond42 ↔ 58 Ref.1
Disulfide bond136 ↔ 201 Ref.1
Disulfide bond168 ↔ 182 Ref.1
Disulfide bond191 ↔ 220 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00767 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 678016446FF5FEB5

FASTA24525,755
        10         20         30         40         50         60 
CGVPAIQPVL SGLARIVNGE DAVPGSWPWQ VSLQDSTGFH FCGGSLISED WVVTAAHCGV 

        70         80         90        100        110        120 
TTSDVVVAGE FDQGLETEDT QVLKIGKVFK NPKFSILTVR NDITLLKLAT PAQFSETVSA 

       130        140        150        160        170        180 
VCLPSADEDF PAGMLCATTG WGKTKYNALK TPDKLQQATL PIVSNTDCRK YWGSRVTDVM 

       190        200        210        220        230        240 
ICAGASGVSS CMGDSGGPLV CQKNGAWTLA GIVSWGSSTC STSTPAVYAR VTALMPWVQE 


TLAAN 

« Hide

References

[1]"Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen."
Smillie L.B., Furka A., Nagabhushan N., Stevenson K.J., Parkes C.O.
Nature 218:343-346(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRKYBOB. A00953.
UniGeneBt.107724.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CBWX-ray2.60A/F1-13[»]
1HJAX-ray2.30A1-13[»]
3BG4X-ray2.50A1-13[»]
ProteinModelPortalP00767.
SMRP00767. Positions 1-245.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00767.
ChEMBLCHEMBL3063.

Protein family/group databases

MEROPSS01.152.

Proteomic databases

PRIDEP00767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG013304.
InParanoidP00767.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00767.

Entry information

Entry nameCTRB_BOVIN
AccessionPrimary (citable) accession number: P00767
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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