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Reviewed, UniProtKB/Swiss-Prot Q00871 (CTRB1_LITVA)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chymotrypsin BI
    EC=3.4.21.1
OrganismLitopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei)
Taxonomic identifier6689 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaDendrobranchiataPenaeoideaPenaeidaeLitopenaeus

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: 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

Signal peptide1 – 1515 Potential
Propeptide16 – 4530Activation peptide Ref.2
PRO_0000027650
Chain46 – 271226Chymotrypsin BI
PRO_0000027651

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
Q00871-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 0967398D5401E5B7

FASTA27128,685
        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 NDIALIRLPS PVSLNSNIKT VKLPSSDVSV GTTVTPTGWG RPSDSASGIS 

       190        200        210        220        230        240 
DVLRQVNVPV MTNADCDSVY GIVGDGVVCI DGTGGKSTCN GDSGGPLNLN GMTYGITSFG 

       250        260        270 
SSAGCEKGYP AAFTRVYYYL DWIQQKTGVT 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: 1516690] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 1458841] [Abstract]
Cited for: PROTEIN SEQUENCE OF 46-65, CHARACTERIZATION.
Tissue: Hepatopancreas.

Cross-references

Sequence databases

X66415 mRNA. Translation: CAA47046.1.
PIRS29239.

3D structure databases

HSSPHSSP built from PDB template 1AZZ based on UniProtKB P00771.
SMRQ00871. Positions 46-271.
ModBaseSearch...

Protein family/group databases

MEROPSS01.122.

Enzyme and pathway databases

BRENDA3.4.21.1. 39338.

Family and domain databases

InterProIPR018114. 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]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCTRB1_LITVA
AccessionPrimary (citable) accession number: Q00871
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents