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P84310 (CTR1_LUMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Chymotrypsin LT_CH 1

EC=3.4.21.1
OrganismLumbricus terrestris (Common earthworm)
Taxonomic identifier6398 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaClitellataOligochaetaHaplotaxidaLumbricinaLumbricidaeLumbricinaeLumbricus

Protein attributes

Sequence length19 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Ref.1

Enzyme regulation

Inhibited by the chymotrypsin inhibitor LTCI. Ref.1 Ref.2

Subunit structure

Monomer. Ref.1

Subcellular location

Secretedextracellular space By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Mass spectrometry

Molecular mass is 23126 Da from positions 1 - ?. Determined by ESI. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›19›19Chymotrypsin LT_CH 1
PRO_0000088688

Regions

Domain1 – ›19›19Peptidase S1

Experimental info

Non-terminal residue191

Sequences

Sequence LengthMass (Da)Tools
P84310 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: A2F0179A5281E5F3

FASTA192,042
        10 
VIGGSDTTIG QYPHQLSLR 

« Hide

References

[1]Wojtaszek J., Wilusz T.
Submitted (NOV-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, MASS SPECTROMETRY.
Tissue: Gut.
[2]"LTCI, a novel chymotrypsin inhibitor of the potato I family from the earthworm Lumbricus terrestris. Purification, cDNA cloning, and expression."
Wojtaszek J., Kolaczkowska A., Kowalska J., Nowak K., Wilusz T.
Comp. Biochem. Physiol. 143B:465-472(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameCTR1_LUMTE
AccessionPrimary (citable) accession number: P84310
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries