Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P36178

- CTRB2_LITVA

UniProt

P36178 - CTRB2_LITVA

Protein

Chymotrypsin BII

Gene
N/A
Organism
Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Collagen degradation

    Protein family/group databases

    MEROPSiS01.122.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymotrypsin BII (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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Propeptidei16 – 4530Activation peptide1 PublicationPRO_0000027652Add
    BLAST
    Chaini46 – 271226Chymotrypsin BIIPRO_0000027653Add
    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

    ProteinModelPortaliP36178.
    SMRiP36178. 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.

    P36178-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV    50
    EATPHSWPHQ AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA 100
    HNIRQNEASQ VSITSTDFFT HENWNSWLLT NDIALIKLPS PVSLNSNIKT 150
    VKLPSSDVAV GTTVTPTGWG RPLDSAGGIS DVLRQVDVPI MTNDDCDAVY 200
    GIVGNGVVCI DSEGGKGTCN GDSGGPLNLN GMTYGITSFG SSAGCEVGYP 250
    DAFTRVYYYL DWIEQKTGVT P 271
    Length:271
    Mass (Da):28,723
    Last modified:June 1, 1994 - v1
    Checksum:i2254D7C7E63FA2E1
    GO

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P36178.
    SMRi P36178. Positions 46-271.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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.
      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 nameiCTRB2_LITVA
    AccessioniPrimary (citable) accession number: P36178
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 73 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