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Protein

Cathepsin L-like proteinase

Gene

Cat-1

Organism
Fasciola hepatica (Liver fluke)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol protease. Probably involved in interaction with host tissues.1 Publication1 Publication

Catalytic activityi

Similar that of papain. Has high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.1 Publication

Enzyme regulationi

Strongly inhibited by Antipain, E64 and Leupeptin, and weakly inhibited by iodoacetic acid (IAA) and phenylmethylsulfonyl fluoride (PMSF). Requires the presence of dithiothreitol (DTT) for activity.1 Publication

Kineticsi

  1. KM=46 µM for Z-Phe-Arg-NHMec (at pH 7.45)1 Publication

    pH dependencei

    Optimum pH is 7-9 in a mixed-buffer system. In a Tris buffer high levels of activity were detected at very alkaline pHs.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei132 – 1321By similarity
    Active sitei269 – 2691By similarity
    Active sitei289 – 2891By similarity

    GO - Molecular functioni

    • cysteine-type endopeptidase activity Source: UniProtKB
    • endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • proteolysis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.B49. 2230.
    3.4.22.B60. 2230.

    Protein family/group databases

    MEROPSiC01.033.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin L-like proteinase (EC:3.4.22.-)
    Gene namesi
    Name:Cat-11 Publication
    OrganismiFasciola hepatica (Liver fluke)
    Taxonomic identifieri6192 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaPlagiorchiidaEchinostomataEchinostomatoideaFasciolidaeFasciola

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence analysisAdd
    BLAST
    Propeptidei16 – 10691Activation peptideSequence analysis1 PublicationPRO_0000042858Add
    BLAST
    Chaini107 – 326220Cathepsin L-like proteinase1 PublicationPRO_0000042859Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei109 – 10913-hydroxyproline; partial1 Publication
    Disulfide bondi129 ↔ 172By similarity
    Disulfide bondi163 ↔ 204By similarity
    Modified residuei196 – 19613-hydroxyproline; partial1 Publication
    Disulfide bondi262 ↔ 311By similarity

    Post-translational modificationi

    Contains cysteine residues involved in intramolecular disulfide bonding.1 Publication

    Keywords - PTMi

    Disulfide bond, Hydroxylation, Zymogen

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 2811Combined sources
    Helixi34 – 5926Combined sources
    Beta strandi62 – 676Combined sources
    Turni71 – 744Combined sources
    Helixi77 – 848Combined sources
    Helixi91 – 944Combined sources
    Beta strandi97 – 1004Combined sources
    Helixi114 – 1174Combined sources
    Helixi132 – 14918Combined sources
    Helixi157 – 1637Combined sources
    Helixi165 – 1673Combined sources
    Helixi171 – 1733Combined sources
    Helixi177 – 1848Combined sources
    Turni192 – 1943Combined sources
    Helixi208 – 2103Combined sources
    Beta strandi213 – 2219Combined sources
    Helixi226 – 23611Combined sources
    Beta strandi239 – 2435Combined sources
    Helixi247 – 2504Combined sources
    Beta strandi252 – 2576Combined sources
    Beta strandi269 – 27911Combined sources
    Beta strandi282 – 2887Combined sources
    Beta strandi300 – 3045Combined sources
    Beta strandi306 – 3094Combined sources
    Helixi310 – 3123Combined sources
    Turni313 – 3153Combined sources
    Beta strandi316 – 3249Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O6XX-ray1.40A17-326[»]
    ProteinModelPortaliQ24940.
    SMRiQ24940. Positions 17-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ24940.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q24940-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRLFILAVLT VGVLGSNDDL WHQWKRMYNK EYNGADDQHR RNIWEKNVKH
    60 70 80 90 100
    IQEHNLRHDL GLVTYTLGLN QFTDMTFEEF KAKYLTEMSR ASDILSHGVP
    110 120 130 140 150
    YEANNRAVPD KIDWRESGYV TEVKDQGNCG SCWAFSTTGT MEGQYMKNER
    160 170 180 190 200
    TSISFSEQQL VDCSGPWGNN GCSGGLMENA YQYLKQFGLE TESSYPYTAV
    210 220 230 240 250
    EGQCRYNKQL GVAKVTGYYT VHSGSEVELK NLVGARRPAA VAVDVESDFM
    260 270 280 290 300
    MYRSGIYQSQ TCSPLRVNHA VLAVGYGTQG GTDYWIVKNS WGTYWGERGY
    310 320
    IRMARNRGNM CGIASLASLP MVARFP
    Length:326
    Mass (Da):36,896
    Last modified:November 1, 1996 - v1
    Checksum:i7FDDB3094D3134A6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L33771 mRNA. Translation: AAA29136.1.
    PIRiS43991.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L33771 mRNA. Translation: AAA29136.1.
    PIRiS43991.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O6XX-ray1.40A17-326[»]
    ProteinModelPortaliQ24940.
    SMRiQ24940. Positions 17-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiC01.033.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.4.22.B49. 2230.
    3.4.22.B60. 2230.

    Miscellaneous databases

    EvolutionaryTraceiQ24940.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCATLL_FASHE
    AccessioniPrimary (citable) accession number: Q24940
    Secondary accession number(s): P91727
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1996
    Last modified: September 7, 2016
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Caution

    It is not clear whether the mature peptide starts at Ala-107 or at Val-108.Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    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 one 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.