CEL2A_PIG
ID CEL2A_PIG Reviewed; 269 AA.
AC P08419;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 145.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3646943; DOI=10.1089/dna.1987.6.163;
RA Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
RT "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs
RT are expressed in human pancreas.";
RL DNA 6:163-172(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834346; DOI=10.1093/oxfordjournals.jbchem.a122204;
RA Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y.,
RA Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y., Tanaka J.,
RA Ikenaga H.;
RT "Molecular cloning and expression in Escherichia coli of a cDNA encoding
RT human pancreatic elastase 2.";
RL J. Biochem. 102:1555-1563(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-269 IN COMPLEX WITH INHIBITOR,
RP AND DISULFIDE BONDS.
RA Jhoti H., Singh O.M.P., Wonacott A.;
RT "Structure of porcine pancreatic elastase complexed with the elastase
RT inhibitor GR143783.";
RL Submitted (AUG-1999) to the PDB data bank.
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; M16651; AAA31027.1; -; mRNA.
DR EMBL; D00237; BAA00166.1; -; mRNA.
DR PIR; A26823; A26823.
DR RefSeq; NP_999274.1; NM_214109.1.
DR PDB; 1BRU; X-ray; 2.30 A; P=29-269.
DR PDBsum; 1BRU; -.
DR AlphaFoldDB; P08419; -.
DR SMR; P08419; -.
DR STRING; 9823.ENSSSCP00000003756; -.
DR BindingDB; P08419; -.
DR ChEMBL; CHEMBL2407; -.
DR MEROPS; S01.155; -.
DR PaxDb; P08419; -.
DR PRIDE; P08419; -.
DR Ensembl; ENSSSCT00000003844; ENSSSCP00000003756; ENSSSCG00000003459.
DR Ensembl; ENSSSCT00015008561; ENSSSCP00015003454; ENSSSCG00015006425.
DR Ensembl; ENSSSCT00025020625; ENSSSCP00025008470; ENSSSCG00025015386.
DR Ensembl; ENSSSCT00045061101; ENSSSCP00045042921; ENSSSCG00045035588.
DR Ensembl; ENSSSCT00070059036; ENSSSCP00070050247; ENSSSCG00070029390.
DR GeneID; 397197; -.
DR KEGG; ssc:397197; -.
DR CTD; 63036; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P08419; -.
DR OMA; GSTLGCN; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF330455; -.
DR Reactome; R-SSC-6809371; Formation of the cornified envelope.
DR EvolutionaryTrace; P08419; -.
DR PRO; PR:P08419; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000003459; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P08419; differential.
DR Genevisible; P08419; SS.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT PROPEP 17..28
FT /note="Activation peptide"
FT /id="PRO_0000027689"
FT CHAIN 29..269
FT /note="Chymotrypsin-like elastase family member 2A"
FT /id="PRO_0000027690"
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 ACT_SITE 121
FT /note="Charge relay system"
FT ACT_SITE 216
FT /note="Charge relay system"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|Ref.3"
FT DISULFID 155..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|Ref.3"
FT DISULFID 186..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|Ref.3"
FT DISULFID 212..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|Ref.3"
FT CONFLICT 10
FT /note="L -> S (in Ref. 2; BAA00166)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="N -> K (in Ref. 2; BAA00166)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="S -> Y (in Ref. 2; BAA00166)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="I -> V (in Ref. 2; BAA00166)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="C -> V (in Ref. 2; BAA00166)"
FT /evidence="ECO:0000305"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1BRU"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1BRU"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1BRU"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:1BRU"
SQ SEQUENCE 269 AA; 28699 MW; BAC6FE69AF4DDE56 CRC64;
MIRALLLSTL VAGALSCGLP ANLPQLPRVV GGEDARPNSW PWQVSLQYDS SGQWRHTCGG
TLVDQSWVLT AAHCISSSRT YRVVLGRHSL STNEPGSLAV KVSKLVVHQD WNSNQLSNGN
DIALLKLASP VSLTDKIQLG CLPAAGTILP NNYVCYVTGW GRLQTNGASP DILQQGQLLV
VDYATCSKPG WWGSTVKTNM ICAGGDGIIS SCNGDSGGPL NCQGANGQWQ VHGIVSFGSS
LGCNYYHKPS VFTRVSNYID WINSVIANN
