CELA1_RAT
ID CELA1_RAT Reviewed; 266 AA.
AC P00773;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chymotrypsin-like elastase family member 1;
DE EC=3.4.21.36;
DE AltName: Full=Elastase-1;
DE Flags: Precursor;
GN Name=Cela1; Synonyms=Ela1;
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 [GENOMIC DNA].
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).
RN [3]
RP PROTEIN SEQUENCE OF 17-45.
RC TISSUE=Pancreas;
RX PubMed=6555050; DOI=10.1021/bi00285a008;
RA Largman C.;
RT "Isolation and characterization of rat pancreatic elastase.";
RL Biochemistry 22:3763-3770(1983).
CC -!- FUNCTION: Acts upon elastin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including elastin. Preferential
CC cleavage: Ala-|-Xaa.; EC=3.4.21.36;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
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; V01234; CAA24544.1; -; mRNA.
DR EMBL; L00117; AAA98811.1; -; Genomic_DNA.
DR EMBL; L00112; AAA98811.1; JOINED; Genomic_DNA.
DR EMBL; L00113; AAA98811.1; JOINED; Genomic_DNA.
DR EMBL; L00114; AAA98811.1; JOINED; Genomic_DNA.
DR EMBL; L00115; AAA98811.1; JOINED; Genomic_DNA.
DR EMBL; L00116; AAA98811.1; JOINED; Genomic_DNA.
DR PIR; A00960; ELRT1.
DR RefSeq; NP_036684.1; NM_012552.4.
DR AlphaFoldDB; P00773; -.
DR SMR; P00773; -.
DR STRING; 10116.ENSRNOP00000006351; -.
DR MEROPS; S01.153; -.
DR PaxDb; P00773; -.
DR PRIDE; P00773; -.
DR GeneID; 24331; -.
DR KEGG; rno:24331; -.
DR UCSC; RGD:2547; rat.
DR CTD; 1990; -.
DR RGD; 2547; Cela1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P00773; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00773; -.
DR TreeFam; TF330455; -.
DR PRO; PR:P00773; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0055123; P:digestive system development; ISO:RGD.
DR GO; GO:0060309; P:elastin catabolic process; ISO:RGD.
DR GO; GO:0031017; P:exocrine pancreas development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0061113; P:pancreas morphogenesis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0048771; P:tissue remodeling; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:6555050"
FT PROPEP 17..26
FT /note="Activation peptide"
FT /id="PRO_0000027683"
FT CHAIN 27..266
FT /note="Chymotrypsin-like elastase family member 1"
FT /id="PRO_0000027684"
FT DOMAIN 27..264
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 56..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 153..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 210..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 104
FT /note="M -> V (in Ref. 2; AAA98811)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> N (in Ref. 2; AAA98811)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> R (in Ref. 2; AAA98811)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="T -> N (in Ref. 2; AAA98811)"
FT /evidence="ECO:0000305"
SQ 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
