ID   CEL2A_BOVIN             Reviewed;         269 AA.
AC   Q29461;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Chymotrypsin-like elastase family member 2A;
DE            EC=3.4.21.71;
DE   AltName: Full=Elastase II;
DE   AltName: Full=Elastase-2;
DE   AltName: Full=Elastase-2A;
DE   Flags: Precursor;
GN   Name=CELA2A; Synonyms=ELA2, ELA2A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=9418008; DOI=10.1016/s0305-0491(97)00031-x;
RA   Gestin M., le Huerou-Luron I., Wicker-Planquart C., le Drean G.,
RA   Chaix J.-C., Puigserver A., Guilloteau P.;
RT   "Bovine pancreatic preproelastases I and II: comparison of nucleotide and
RT   amino acid sequences and tissue specific expression.";
RL   Comp. Biochem. Physiol. 118B:181-187(1997).
CC   -!- FUNCTION: Elastase that enhances insulin signaling and might have a
CC       physiologic role in cellular glucose metabolism. Circulates in plasma
CC       and reduces platelet hyperactivation, triggers both insulin secretion
CC       and degradation, and increases insulin sensitivity.
CC       {ECO:0000250|UniProtKB:P08217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa.
CC         Hydrolyzes elastin.; EC=3.4.21.71;
CC         Evidence={ECO:0000250|UniProtKB:P08217};
CC   -!- SUBUNIT: Interacts with CPA1. Interacts with SERPINA1.
CC       {ECO:0000250|UniProtKB:P08217}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08217}.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; X97635; CAA66231.1; -; mRNA.
DR   RefSeq; NP_777139.1; NM_174714.2.
DR   AlphaFoldDB; Q29461; -.
DR   SMR; Q29461; -.
DR   STRING; 9913.ENSBTAP00000033941; -.
DR   MEROPS; S01.155; -.
DR   PaxDb; Q29461; -.
DR   GeneID; 282687; -.
DR   KEGG; bta:282687; -.
DR   CTD; 63036; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q29461; -.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:1901143; P:insulin catabolic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR   GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
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; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   PROPEP          17..28
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027685"
FT   CHAIN           29..269
FT                   /note="Chymotrypsin-like elastase family member 2A"
FT                   /id="PRO_0000027686"
FT   DOMAIN          29..267
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        73
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        121
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        155..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        186..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        212..243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   269 AA;  28857 MW;  8343B97062CF267C CRC64;
     MIRALLLSTL VAGALSCGVP TYPPQLSRVV GGEDARPNSW PWQVSLQYSS SGQWRHTCGG
     SLIEQNWVLT AAHCISSSRT YRVVVGRQSL STVESGSLTI AVSKSVIHEK WNSNQLAQGN
     DIALLKLASS VPLTDKIQLG CLPAAGTILP NNYVCYVTGW GRLQSNGALP DILQQGKLLV
     VDYATCSNPS WWGSTVKTNM ICAGGDGVTS SCNGDSGGPL NCQAANRQWQ VHGIVSFGSS
     LGCNYYRKPS VFTRVSNYND WISSVIENN