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Chymotrypsin-like elastase family member 2A (EC 3.4.21.71) (Elastase-2) (Elastase-2A)

 CEL2A_PIG               Reviewed;         269 AA.
P08419;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-FEB-2018, entry version 128.
RecName: Full=Chymotrypsin-like elastase family member 2A;
EC=3.4.21.71;
AltName: Full=Elastase-2;
AltName: Full=Elastase-2A;
Flags: Precursor;
Name=CELA2A; Synonyms=ELA2, ELA2A;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3646943; DOI=10.1089/dna.1987.6.163;
Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
"Characterization of pancreatic elastase II cDNAs: two elastase II
mRNAs are expressed in human pancreas.";
DNA 6:163-172(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2834346;
Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y.,
Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y.,
Tanaka J., Ikenaga H.;
"Molecular cloning and expression in Escherichia coli of a cDNA
encoding human pancreatic elastase 2.";
J. Biochem. 102:1555-1563(1987).
[3]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-269 IN COMPLEX WITH
INHIBITOR, AND DISULFIDE BONDS.
Jhoti H., Singh O.M.P., Wonacott A.;
"Structure of porcine pancreatic elastase complexed with the elastase
inhibitor GR143783.";
Submitted (AUG-1999) to the PDB data bank.
-!- FUNCTION: Acts upon elastin.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
and Phe-|-Xaa. Hydrolyzes elastin.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Pancreas.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M16651; AAA31027.1; -; mRNA.
EMBL; D00237; BAA00166.1; -; mRNA.
PIR; A26823; A26823.
RefSeq; NP_999274.1; NM_214109.1.
UniGene; Ssc.316; -.
PDB; 1BRU; X-ray; 2.30 A; P=29-269.
PDBsum; 1BRU; -.
ProteinModelPortal; P08419; -.
SMR; P08419; -.
STRING; 9823.ENSSSCP00000003756; -.
BindingDB; P08419; -.
ChEMBL; CHEMBL2407; -.
MEROPS; S01.155; -.
PaxDb; P08419; -.
PRIDE; P08419; -.
Ensembl; ENSSSCT00000003844; ENSSSCP00000003756; ENSSSCG00000003459.
GeneID; 397197; -.
KEGG; ssc:397197; -.
CTD; 63036; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119027; -.
InParanoid; P08419; -.
KO; K01346; -.
OMA; KIQLGCL; -.
OrthoDB; EOG091G0DF7; -.
TreeFam; TF330455; -.
Reactome; R-SSC-6809371; Formation of the cornified envelope.
EvolutionaryTrace; P08419; -.
PRO; PR:P08419; -.
Proteomes; UP000008227; Chromosome 6.
Bgee; ENSSSCG00000003459; -.
Genevisible; P08419; SS.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Hydrolase; Protease;
Reference proteome; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 16
PROPEP 17 28 Activation peptide.
/FTId=PRO_0000027689.
CHAIN 29 269 Chymotrypsin-like elastase family member
2A.
/FTId=PRO_0000027690.
DOMAIN 29 267 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system.
ACT_SITE 121 121 Charge relay system.
ACT_SITE 216 216 Charge relay system.
DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|Ref.3}.
DISULFID 155 222 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|Ref.3}.
DISULFID 186 202 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|Ref.3}.
DISULFID 212 243 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|Ref.3}.
CONFLICT 10 10 L -> S (in Ref. 2; BAA00166).
{ECO:0000305}.
CONFLICT 118 118 N -> K (in Ref. 2; BAA00166).
{ECO:0000305}.
CONFLICT 132 132 S -> Y (in Ref. 2; BAA00166).
{ECO:0000305}.
CONFLICT 172 172 I -> V (in Ref. 2; BAA00166).
{ECO:0000305}.
CONFLICT 202 202 C -> V (in Ref. 2; BAA00166).
{ECO:0000305}.
STRAND 43 50 {ECO:0000244|PDB:1BRU}.
STRAND 53 64 {ECO:0000244|PDB:1BRU}.
STRAND 67 70 {ECO:0000244|PDB:1BRU}.
HELIX 72 74 {ECO:0000244|PDB:1BRU}.
STRAND 81 86 {ECO:0000244|PDB:1BRU}.
STRAND 88 92 {ECO:0000244|PDB:1BRU}.
STRAND 98 107 {ECO:0000244|PDB:1BRU}.
HELIX 116 118 {ECO:0000244|PDB:1BRU}.
STRAND 123 129 {ECO:0000244|PDB:1BRU}.
STRAND 154 160 {ECO:0000244|PDB:1BRU}.
STRAND 174 181 {ECO:0000244|PDB:1BRU}.
HELIX 183 186 {ECO:0000244|PDB:1BRU}.
TURN 189 192 {ECO:0000244|PDB:1BRU}.
HELIX 193 195 {ECO:0000244|PDB:1BRU}.
STRAND 200 203 {ECO:0000244|PDB:1BRU}.
STRAND 206 210 {ECO:0000244|PDB:1BRU}.
STRAND 219 223 {ECO:0000244|PDB:1BRU}.
STRAND 229 237 {ECO:0000244|PDB:1BRU}.
STRAND 242 244 {ECO:0000244|PDB:1BRU}.
STRAND 250 254 {ECO:0000244|PDB:1BRU}.
HELIX 255 257 {ECO:0000244|PDB:1BRU}.
HELIX 259 268 {ECO:0000244|PDB:1BRU}.
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


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