ID   ELAS_GADMO              Reviewed;          20 AA.
AC   P32197;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Elastase;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Intestine;
RX   PubMed=8518301; DOI=10.1016/0167-4838(93)90116-9;
RA   Asgeirsson B., Bjarnason J.B.;
RT   "Properties of elastase from Atlantic cod, a cold-adapted proteinase.";
RL   Biochim. Biophys. Acta 1164:91-100(1993).
CC   -!- FUNCTION: Digests most rapidly at the C-terminal side of alanine
CC       residues, but also cleaves at valine and leucine residues.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   PIR; S33787; S33787.
DR   AlphaFoldDB; P32197; -.
DR   MEROPS; S01.153; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..>20
FT                   /note="Elastase"
FT                   /id="PRO_0000088678"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2284 MW;  51D4B08262AC84BC CRC64;
     VVGGEVARAH SWPWQISLQY