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O17473 (CATL_BRUPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:
Cathepsin L-like

EC=3.4.22.15
OrganismBrugia pahangi (Filarial nematode worm)
Taxonomic identifier6280 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 181165Activation peptide Potential
PRO_0000026293
Chain182 – 395214Cathepsin L-like
PRO_0000026294

Sites

Active site2061 By similarity
Active site3421 By similarity
Active site3631 By similarity

Amino acid modifications

Disulfide bond203 ↔ 246 Ref.2
Disulfide bond237 ↔ 278 Ref.2
Disulfide bond337 ↔ 385 Ref.2

Secondary structure

................................ 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O17473 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 6EC65C20333BE2D1

FASTA39544,549
        10         20         30         40         50         60 
MWTIAQLAVF AILALADFAV AGEIEQLKEV LGKFNKDYKQ GNMTRLASDF RSALKEYGDG 

        70         80         90        100        110        120 
QQGESTVVQE FLKKTEDNGE QRAMEKLETE WKDYVTALGK HYDQKENNFR MAIFESNELM 

       130        140        150        160        170        180 
TERINKKYEQ GLVSYTTALN DLADLTDEEF MVRNGLRLPN QTDLRGKRQT SEFYRYDKSE 

       190        200        210        220        230        240 
RLPDQVDWRT KGAVTPVRNQ GECGSCYAFA TAAALEAYHK QMTGRLLDLS PQNIVDCTRN 

       250        260        270        280        290        300 
LGNNGCSGGY MPTAFQYASR YGIAMESRYP YVGTEQRCRW QQSIAVVTDN GFNEIQPGDE 

       310        320        330        340        350        360 
LALKHAVAKR GPVVVGISGS KRSFRFYKDG VYSEGNCGRP DHAVLAVGYG THPSYGDYWI 

       370        380        390 
VKNSWGTDWG KDGYVYMARN RGNMCHIASA ASFPI 

« Hide

References

[1]"Cathepsin L-like cysteine protease from Brugia pahangi third stage larvae."
Selzer P.M., Huong X., Britton C., McKerrow J.H.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular model of Brugia pahangi third-stage larvae cysteine protease."
Selzer P.M., Chen X., Cohen F.E., McKerrow J.H.
Submitted (JUL-1998) to the PDB data bank
Cited for: 3D-STRUCTURE MODELING OF 182-395, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031819 mRNA. Translation: AAB86867.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMUmodel-A182-395[»]
ProteinModelPortalO17473.
SMRO17473. Positions 182-395.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATL_BRUPA
AccessionPrimary (citable) accession number: O17473
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 70 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references