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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)DescriptionActionsGraphical viewLength
    Active sitei132By similarity1
    Active sitei269By similarity1
    Active sitei289By similarity1

    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 15Sequence analysisAdd BLAST15
    PropeptideiPRO_000004285816 – 106Activation peptideSequence analysis1 PublicationAdd BLAST91
    ChainiPRO_0000042859107 – 326Cathepsin L-like proteinase1 PublicationAdd BLAST220

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1093-hydroxyproline; partial1 Publication1
    Disulfide bondi129 ↔ 172By similarity
    Disulfide bondi163 ↔ 204By similarity
    Modified residuei1963-hydroxyproline; partial1 Publication1
    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

    1326
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi18 – 28Combined sources11
    Helixi34 – 59Combined sources26
    Beta strandi62 – 67Combined sources6
    Turni71 – 74Combined sources4
    Helixi77 – 84Combined sources8
    Helixi91 – 94Combined sources4
    Beta strandi97 – 100Combined sources4
    Helixi114 – 117Combined sources4
    Helixi132 – 149Combined sources18
    Helixi157 – 163Combined sources7
    Helixi165 – 167Combined sources3
    Helixi171 – 173Combined sources3
    Helixi177 – 184Combined sources8
    Turni192 – 194Combined sources3
    Helixi208 – 210Combined sources3
    Beta strandi213 – 221Combined sources9
    Helixi226 – 236Combined sources11
    Beta strandi239 – 243Combined sources5
    Helixi247 – 250Combined sources4
    Beta strandi252 – 257Combined sources6
    Beta strandi269 – 279Combined sources11
    Beta strandi282 – 288Combined sources7
    Beta strandi300 – 304Combined sources5
    Beta strandi306 – 309Combined sources4
    Helixi310 – 312Combined sources3
    Turni313 – 315Combined sources3
    Beta strandi316 – 324Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2O6XX-ray1.40A17-326[»]
    ProteinModelPortaliQ24940.
    SMRiQ24940.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2O6XX-ray1.40A17-326[»]
    ProteinModelPortaliQ24940.
    SMRiQ24940.
    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: November 2, 2016
    This is version 70 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.