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P36178 (CTRB2_LITVA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. 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 attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease with chymotryptic and collagenolytic activities.

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 processCollagen degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

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

Signal peptide1 – 1515 Potential
Propeptide16 – 4530Activation peptide
PRO_0000027652
Chain46 – 271226Chymotrypsin BII
PRO_0000027653

Regions

Domain46 – 268223Peptidase S1

Sites

Active site861Charge relay system By similarity
Active site1321Charge relay system By similarity
Active site2231Charge relay system By similarity

Amino acid modifications

Disulfide bond71 ↔ 87 By similarity
Disulfide bond196 ↔ 209 By similarity
Disulfide bond219 ↔ 245 By similarity

Sequences

Sequence LengthMass (Da)Tools
P36178 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 2254D7C7E63FA2E1

FASTA27128,723
        10         20         30         40         50         60 
MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV EATPHSWPHQ 

        70         80         90        100        110        120 
AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA HNIRQNEASQ VSITSTDFFT 

       130        140        150        160        170        180 
HENWNSWLLT NDIALIKLPS PVSLNSNIKT VKLPSSDVAV GTTVTPTGWG RPLDSAGGIS 

       190        200        210        220        230        240 
DVLRQVDVPI MTNDDCDAVY GIVGNGVVCI DSEGGKGTCN GDSGGPLNLN GMTYGITSFG 

       250        260        270 
SSAGCEVGYP DAFTRVYYYL DWIEQKTGVT P 

« Hide

References

[1]"Molecular cloning of a cDNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vanameii (Crustacea, Decapoda)."
Sellos D., van Wormhoudt A.
FEBS Lett. 309:219-224(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Hepatopancreas.
[2]"Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda)."
van Wormhoudt A., le Chevalier P., Sellos D.
Comp. Biochem. Physiol. 103B:675-680(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 46-65, CHARACTERIZATION.
Tissue: Hepatopancreas.

Cross-references

3D structure databases

ProteinModelPortalP36178.
SMRP36178. Positions 46-271.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameCTRB2_LITVA
AccessionPrimary (citable) accession number: P36178
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 16, 2013
This is version 71 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