ID   CEL2A_RAT               Reviewed;         271 AA.
AC   P00774;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Chymotrypsin-like elastase family member 2A;
DE            EC=3.4.21.71;
DE   AltName: Full=Elastase-2;
DE   AltName: Full=Elastase-2A;
DE   Flags: Precursor;
GN   Name=Cela2a; Synonyms=Ela2, Ela2a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6918221; DOI=10.1021/bi00535a053;
RA   MacDonald R.J., Swift G.H., Quinto C., Swain W., Pictet R.L., Nikovits W.,
RA   Rutter W.J.;
RT   "Primary structure of two distinct rat pancreatic preproelastases
RT   determined by sequence analysis of the complete cloned messenger
RT   ribonucleic acid sequences.";
RL   Biochemistry 21:1453-1463(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6094548; DOI=10.1016/s0021-9258(18)89888-x;
RA   Swift G.H., Craik C.S., Stary S.J., Quinto C., Lahaie R.G., Rutter W.J.,
RA   MacDonald R.J.;
RT   "Structure of the two related elastase genes expressed in the rat
RT   pancreas.";
RL   J. Biol. Chem. 259:14271-14278(1984).
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; V01233; CAA24543.1; -; mRNA.
DR   EMBL; L00124; AAA98780.1; -; Genomic_DNA.
DR   EMBL; L00118; AAA98780.1; JOINED; Genomic_DNA.
DR   EMBL; L00119; AAA98780.1; JOINED; Genomic_DNA.
DR   EMBL; L00120; AAA98780.1; JOINED; Genomic_DNA.
DR   EMBL; L00121; AAA98780.1; JOINED; Genomic_DNA.
DR   EMBL; L00122; AAA98780.1; JOINED; Genomic_DNA.
DR   EMBL; L00123; AAA98780.1; JOINED; Genomic_DNA.
DR   PIR; A00961; ELRT2.
DR   RefSeq; NP_036685.1; NM_012553.2.
DR   AlphaFoldDB; P00774; -.
DR   SMR; P00774; -.
DR   STRING; 10116.ENSRNOP00000018349; -.
DR   BindingDB; P00774; -.
DR   ChEMBL; CHEMBL3888; -.
DR   MEROPS; S01.155; -.
DR   PhosphoSitePlus; P00774; -.
DR   PaxDb; P00774; -.
DR   Ensembl; ENSRNOT00000018349; ENSRNOP00000018349; ENSRNOG00000013628.
DR   GeneID; 24332; -.
DR   KEGG; rno:24332; -.
DR   UCSC; RGD:2548; rat.
DR   CTD; 63036; -.
DR   RGD; 2548; Cela2a.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234528; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; P00774; -.
DR   OMA; GSTLGCN; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P00774; -.
DR   TreeFam; TF330455; -.
DR   Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR   PRO; PR:P00774; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000013628; Expressed in pancreas and 17 other tissues.
DR   Genevisible; P00774; RN.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0036457; C:keratohyalin granule; ISO:RGD.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0017171; F:serine hydrolase activity; ISO:RGD.
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   PROPEP          17..30
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027691"
FT   CHAIN           31..271
FT                   /note="Chymotrypsin-like elastase family member 2A"
FT                   /id="PRO_0000027692"
FT   DOMAIN          31..269
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        123
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        157..224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        188..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        214..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   271 AA;  28885 MW;  125C783B857B71E3 CRC64;
     MIRTLLLSAL VAGALSCGYP TYEVQHDVSR VVGGQEASPN SWPWQVSLQY LSSGKWHHTC
     GGSLVANNWV LTAAHCISNS RTYRVLLGRH SLSTSESGSL AVQVSKLVVH EKWNAQKLSN
     GNDIALVKLA SPVALTSKIQ TACLPPAGTI LPNNYPCYVT GWGRLQTNGA TPDVLQQGRL
     LVVDYATCSS ASWWGSSVKT NMVCAGGDGV TSSCNGDSGG PLNCQASNGQ WQVHGIVSFG
     STLGCNYPRK PSVFTRVSNY IDWINSVIAK N