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O97398

- CTR_PHACE

UniProt

O97398 - CTR_PHACE

Protein

Chymotrypsin

Gene
N/A
Organism
Phaedon cochleariae (Mustard beetle)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Serine protease with chymotryptic and collagenolytic activities.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei89 – 891Charge relay systemBy similarity
    Active sitei135 – 1351Charge relay systemBy similarity
    Active sitei229 – 2291Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Collagen degradation, Digestion

    Protein family/group databases

    MEROPSiS01.082.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymotrypsin (EC:3.4.21.1)
    OrganismiPhaedon cochleariae (Mustard beetle)
    Taxonomic identifieri80249 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaChrysomeloideaChrysomelidaeChrysomelinaeChrysomeliniPhaedon

    Subcellular locationi

    Secretedextracellular space By similarity

    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 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 4529Activation peptideBy similarityPRO_0000314680Add
    BLAST
    Chaini46 – 276231ChymotrypsinSequence AnalysisPRO_5000147324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi74 ↔ 90By similarityPROSITE-ProRule annotation
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi202 ↔ 215By similarityPROSITE-ProRule annotation
    Disulfide bondi225 ↔ 250By similarityPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    Expressed in larval carcasses and gut, and adult gut.1 Publication

    Developmental stagei

    Ovarial and mature eggs, larvae and adult.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO97398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 272227Peptidase 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.

    O97398-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVALVVLAL FGVSLAASID NIEIPPSKNI YVEPINQPEV DPSLEIVNGQ    50
    EVVPHSIPYQ IFLVASAGET SWTCGGSLIT KRYVLTAAHC IQGAKSVHVT 100
    LGAHNLAKHE ASKVTVNGRS WVIHEKYDST NIDNDIGVIQ LERNLTLTRS 150
    IQLARLPSLR DVGINLEGRT ATVSGWGLTN GIFQTTTDVL RANNTIISNK 200
    ECNDVFKIVQ PTEVCLSIAG GRSACSGDSG GPLVIDNVQH GIVSYGSSYC 250
    RSTPSVFTRV SSYLNWLQTH SEWRAQ 276
    Length:276
    Mass (Da):29,868
    Last modified:May 1, 1999 - v1
    Checksum:iFC5FD05DB882A1DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17904 mRNA. Translation: CAA76928.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17904 mRNA. Translation: CAA76928.1 .

    3D structure databases

    ProteinModelPortali O97398.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.082.

    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 cDNAs encoding a range of digestive enzymes from a phytophagous beetle, Phaedon cochleariae."
      Girard C., Jouanin L.
      Insect Biochem. Mol. Biol. 29:1129-1142(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Larval gut1 Publication.

    Entry informationi

    Entry nameiCTR_PHACE
    AccessioniPrimary (citable) accession number: O97398
    Secondary accession number(s): P81521
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    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