ID   CEL3B_MACMU             Reviewed;         257 AA.
AC   O19023;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Chymotrypsin-like elastase family member 3B;
DE            EC=3.4.21.70;
DE   AltName: Full=Elastase IIIB;
DE   AltName: Full=Elastase-3B;
DE   AltName: Full=Protease E;
DE   Flags: Precursor; Fragment;
GN   Name=CELA3B; Synonyms=ELA3B;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RA   Sziegoleit A.;
RT   "Pancreatic elastase from rhesus monkey.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Efficient protease with alanine specificity but only little
CC       elastolytic activity. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.;
CC         EC=3.4.21.70;
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ000067; CAA03899.1; -; mRNA.
DR   AlphaFoldDB; O19023; -.
DR   SMR; O19023; -.
DR   STRING; 9544.ENSMMUP00000005184; -.
DR   MEROPS; S01.154; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; O19023; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          <1..2
FT                   /note="Or 3"
FT                   /evidence="ECO:0000255"
FT   PROPEP          3..15
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027701"
FT   CHAIN           16..>257
FT                   /note="Chymotrypsin-like elastase family member 3B"
FT                   /id="PRO_0000027702"
FT   DOMAIN          16..255
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        60
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        104..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
FT   NON_TER         257
SQ   SEQUENCE   257 AA;  27687 MW;  4D443DB67233D8DC CRC64;
     VASGYGPPSS HPSSRVVNGE DAVPYSWPWQ VSLQYEKNGS FHHTCGGSLI APDWVVTAGH
     CISSSLTYQV ALGDYNLAVK EGPEQVIPIN SGDLFVHPLW NRLCVACGND IALIKLSRSA
     QLGDAVQLAS LPPAGDILPN ETPCYITGWG RLYTNGPLPD KLQRALLPVV DYEHCSKWNW
     WGSTVKKTMV CAGGDIRSGC NGDSGGPLNC PTDDGGWQVH GVTSFVSSFG CNTQRKPTVF
     TRVSAFIDWI EETIASH