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Chymotrypsin-like elastase family member 1 (EC 3.4.21.36) (Elastase-1)

 CELA1_RAT               Reviewed;         266 AA.
P00773;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-DEC-2018, entry version 141.
RecName: Full=Chymotrypsin-like elastase family member 1;
EC=3.4.21.36;
AltName: Full=Elastase-1;
Flags: Precursor;
Name=Cela1; Synonyms=Ela1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6918221; DOI=10.1021/bi00535a053;
MacDonald R.J., Swift G.H., Quinto C., Swain W., Pictet R.L.,
Nikovits W., Rutter W.J.;
"Primary structure of two distinct rat pancreatic preproelastases
determined by sequence analysis of the complete cloned messenger
ribonucleic acid sequences.";
Biochemistry 21:1453-1463(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6094548;
Swift G.H., Craik C.S., Stary S.J., Quinto C., Lahaie R.G.,
Rutter W.J., MacDonald R.J.;
"Structure of the two related elastase genes expressed in the rat
pancreas.";
J. Biol. Chem. 259:14271-14278(1984).
[3]
PROTEIN SEQUENCE OF 17-45.
TISSUE=Pancreas;
PubMed=6555050; DOI=10.1021/bi00285a008;
Largman C.;
"Isolation and characterization of rat pancreatic elastase.";
Biochemistry 22:3763-3770(1983).
-!- FUNCTION: Acts upon elastin.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of proteins, including elastin. Preferential
cleavage: Ala-|-Xaa.; EC=3.4.21.36;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- 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; V01234; CAA24544.1; -; mRNA.
EMBL; L00117; AAA98811.1; -; Genomic_DNA.
EMBL; L00112; AAA98811.1; JOINED; Genomic_DNA.
EMBL; L00113; AAA98811.1; JOINED; Genomic_DNA.
EMBL; L00114; AAA98811.1; JOINED; Genomic_DNA.
EMBL; L00115; AAA98811.1; JOINED; Genomic_DNA.
EMBL; L00116; AAA98811.1; JOINED; Genomic_DNA.
PIR; A00960; ELRT1.
RefSeq; NP_036684.1; NM_012552.4.
UniGene; Rn.6044; -.
ProteinModelPortal; P00773; -.
SMR; P00773; -.
STRING; 10116.ENSRNOP00000006351; -.
MEROPS; S01.153; -.
PaxDb; P00773; -.
PRIDE; P00773; -.
GeneID; 24331; -.
KEGG; rno:24331; -.
UCSC; RGD:2547; rat.
CTD; 1990; -.
RGD; 2547; Cela1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251820; -.
InParanoid; P00773; -.
KO; K01326; -.
PhylomeDB; P00773; -.
TreeFam; TF330455; -.
PRO; PR:P00773; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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;
Calcium; Complete proteome; Direct protein sequencing; Disulfide bond;
Hydrolase; Metal-binding; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 16 {ECO:0000269|PubMed:6555050}.
PROPEP 17 26 Activation peptide.
/FTId=PRO_0000027683.
CHAIN 27 266 Chymotrypsin-like elastase family member
1.
/FTId=PRO_0000027684.
DOMAIN 27 264 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 71 71 Charge relay system. {ECO:0000250}.
ACT_SITE 119 119 Charge relay system. {ECO:0000250}.
ACT_SITE 214 214 Charge relay system. {ECO:0000250}.
METAL 85 85 Calcium. {ECO:0000250}.
METAL 90 90 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 95 95 Calcium. {ECO:0000250}.
DISULFID 56 72 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 153 220 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 184 200 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 210 240 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 104 104 M -> V (in Ref. 2; AAA98811).
{ECO:0000305}.
CONFLICT 108 108 T -> N (in Ref. 2; AAA98811).
{ECO:0000305}.
CONFLICT 244 244 K -> R (in Ref. 2; AAA98811).
{ECO:0000305}.
CONFLICT 266 266 T -> N (in Ref. 2; AAA98811).
{ECO:0000305}.
SEQUENCE 266 AA; 28976 MW; 5A56FE8FCF1AAEDA CRC64;
MLRFLVFASL VLYGHSTQDF PETNARVVGG AEARRNSWPS QISLQYLSGG SWYHTCGGTL
IRRNWVMTAA HCVSSQMTFR VVVGDHNLSQ NDGTEQYVSV QKIMVHPTWN SNNVAAGYDI
ALLRLAQSVT LNNYVQLAVL PQEGTILANN NPCYITGWGR TRTNGQLSQT LQQAYLPSVD
YSICSSSSYW GSTVKTTMVC AGGDGVRSGC QGDSGGPLHC LVNGQYSVHG VTSFVSSMGC
NVSKKPTVFT RVSAYISWMN NVIAYT


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