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Protein

Chymotrypsin BI

Gene
N/A
Organism
Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease with chymotryptic and collagenolytic activities.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Charge relay systemBy similarity
Active sitei132 – 1321Charge relay systemBy similarity
Active sitei223 – 2231Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Collagen degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin BI (EC:3.4.21.1)
OrganismiLitopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei)
Taxonomic identifieri6689 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaDendrobranchiataPenaeoideaPenaeidaeLitopenaeus

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Propeptidei16 – 4530Activation peptide1 PublicationPRO_0000027650Add
BLAST
Chaini46 – 271226Chymotrypsin BIPRO_0000027651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 87PROSITE-ProRule annotation
Disulfide bondi196 ↔ 209PROSITE-ProRule annotation
Disulfide bondi219 ↔ 245PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ00871.
SMRiQ00871. Positions 46-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 268223Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00871-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV
60 70 80 90 100
EATPHSWPHQ AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA
110 120 130 140 150
HNIRQNEASQ VSITSTDFFT HENWNSWLLT NDIALIRLPS PVSLNSNIKT
160 170 180 190 200
VKLPSSDVSV GTTVTPTGWG RPSDSASGIS DVLRQVNVPV MTNADCDSVY
210 220 230 240 250
GIVGDGVVCI DGTGGKSTCN GDSGGPLNLN GMTYGITSFG SSAGCEKGYP
260 270
AAFTRVYYYL DWIQQKTGVT P
Length:271
Mass (Da):28,685
Last modified:February 1, 1994 - v1
Checksum:i0967398D5401E5B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66415 mRNA. Translation: CAA47046.1.
PIRiS29239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66415 mRNA. Translation: CAA47046.1.
PIRiS29239.

3D structure databases

ProteinModelPortaliQ00871.
SMRiQ00871. Positions 46-271.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 46-65, CHARACTERIZATION.
    Tissue: Hepatopancreas.

Entry informationi

Entry nameiCTRB1_LITVA
AccessioniPrimary (citable) accession number: Q00871
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.