CTRL_HALRU
ID CTRL_HALRU Reviewed; 254 AA.
AC P35003;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chymotrypsin-like serine proteinase;
DE EC=3.4.21.-;
DE Flags: Precursor;
OS Haliotis rufescens (California red abalone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=6454;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Gut;
RX PubMed=8342947; DOI=10.1006/abbi.1993.1406;
RA Groppe J.C., Morse D.E.;
RT "Molluscan chymotrypsin-like protease: structure, localization, and
RT substrate specificity.";
RL Arch. Biochem. Biophys. 305:159-169(1993).
CC -!- FUNCTION: Specificity similar to chymotrypsin.
CC -!- ACTIVITY REGULATION: Activated by an autocatalytic mechanism.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the distal quarter of the
CC intestine.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; X71438; CAA50572.1; -; mRNA.
DR PIR; S35585; S35585.
DR AlphaFoldDB; P35003; -.
DR SMR; P35003; -.
DR MEROPS; S01.422; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..23
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027658"
FT CHAIN 24..254
FT /note="Chymotrypsin-like serine proteinase"
FT /id="PRO_0000027659"
FT DOMAIN 24..254
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 53..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 146..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 181..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 208..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 254 AA; 27250 MW; ADAA9A8A22BEFCEC CRC64;
MNALLNILLC TLAATALAEI SPNIVGGSNA AAGEFPWQGS LQVRSGTSWF HICGCVLYTT
SKALTAAHCL SNSASSYRLG FGMLRMNNVD GTEQYSSVTS YTNHPNYNGN AAGYPNDIAV
LRLTSSMDTS SSAVGPSVWL LVERLCRTNM YDQRMGKTQW RWQHPNNLQK VDMTVLTNSD
CSSRWSGISG ATVNSGHICI FESGRSACSG DSGGPLVCGN TLTGITSWGI SSCSGSYPSV
YTRVSSFYNW VQTQ
