ID   CTR1_LUMTE              Reviewed;          19 AA.
AC   P84310;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Chymotrypsin LT_CH 1;
DE            EC=3.4.21.1;
DE   Flags: Fragment;
OS   Lumbricus terrestris (Common earthworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Lumbricus.
OX   NCBI_TaxID=6398;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Gut;
RA   Wojtaszek J., Wilusz T.;
RL   Submitted (NOV-2004) to UniProtKB.
RN   [2] {ECO:0000305}
RP   ACTIVITY REGULATION.
RX   PubMed=16469515; DOI=10.1016/j.cbpb.2005.12.023;
RA   Wojtaszek J., Kolaczkowska A., Kowalska J., Nowak K., Wilusz T.;
RT   "LTCI, a novel chymotrypsin inhibitor of the potato I family from the
RT   earthworm Lumbricus terrestris. Purification, cDNA cloning, and
RT   expression.";
RL   Comp. Biochem. Physiol. 143B:465-472(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC         Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC         ECO:0000255|PROSITE-ProRule:PRU10079, ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Inhibited by the chymotrypsin inhibitor LTCI.
CC       {ECO:0000269|PubMed:16469515, ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=23126; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   AlphaFoldDB; P84310; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..>19
FT                   /note="Chymotrypsin LT_CH 1"
FT                   /id="PRO_0000088688"
FT   DOMAIN          1..>19
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         19
SQ   SEQUENCE   19 AA;  2042 MW;  A2F0179A5281E5F3 CRC64;
     VIGGSDTTIG QYPHQLSLR