ID   ELA2A_BOVIN             Reviewed;         269 AA.
AC   Q29461;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Elastase-2A;
DE            EC=3.4.21.71;
DE   AltName: Full=Elastase-2;
DE   AltName: Full=Elastase II;
DE   Flags: Precursor;
GN   Name=ELA2A; Synonyms=ELA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   MEDLINE=98079203; PubMed=9418008; DOI=10.1016/S0305-0491(97)00031-X;
RA   Gestin M., le Huerou-Luron I., Wicker-Planquart C., le Drean G.,
RA   Chaix J.-C., Puigserver A., Guilloteau P.;
RT   "Bovine pancreatic preproelastases I and II: comparison of nucleotide
RT   and amino acid sequences and tissue specific expression.";
RL   Comp. Biochem. Physiol. 118B:181-187(1997).
CC   -!- FUNCTION: Acts upon elastin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
CC       and Phe-|-Xaa. Hydrolyzes elastin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; X97635; CAA66231.1; -; mRNA.
DR   IPI; IPI00687568; -.
DR   RefSeq; NP_777139.1; -.
DR   UniGene; Bt.311; -.
DR   HSSP; P08419; 1BRU.
DR   SMR; Q29461; 29-269.
DR   MEROPS; S01.155; -.
DR   Ensembl; ENSBTAG00000024496; Bos taurus.
DR   GeneID; 282687; -.
DR   KEGG; bta:282687; -.
DR   HOVERGEN; Q29461; -.
DR   BRENDA; 3.4.21.71; 251.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     16       By similarity.
FT   PROPEP       17     28       Activation peptide (By similarity).
FT                                /FTId=PRO_0000027685.
FT   CHAIN        29    269       Elastase-2A.
FT                                /FTId=PRO_0000027686.
FT   DOMAIN       29    267       Peptidase S1.
FT   ACT_SITE     73     73       Charge relay system (By similarity).
FT   ACT_SITE    121    121       Charge relay system (By similarity).
FT   ACT_SITE    216    216       Charge relay system (By similarity).
FT   DISULFID     58     74       By similarity.
FT   DISULFID    155    222       By similarity.
FT   DISULFID    186    202       By similarity.
FT   DISULFID    212    243       By similarity.
SQ   SEQUENCE   269 AA;  28857 MW;  8343B97062CF267C CRC64;
     MIRALLLSTL VAGALSCGVP TYPPQLSRVV GGEDARPNSW PWQVSLQYSS SGQWRHTCGG
     SLIEQNWVLT AAHCISSSRT YRVVVGRQSL STVESGSLTI AVSKSVIHEK WNSNQLAQGN
     DIALLKLASS VPLTDKIQLG CLPAAGTILP NNYVCYVTGW GRLQSNGALP DILQQGKLLV
     VDYATCSNPS WWGSTVKTNM ICAGGDGVTS SCNGDSGGPL NCQAANRQWQ VHGIVSFGSS
     LGCNYYRKPS VFTRVSNYND WISSVIENN
//