ID   ELA1_BOVIN              Reviewed;         266 AA.
AC   Q28153; A6QPW5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Elastase-1;
DE            EC=3.4.21.36;
DE   AltName: Full=Elastase I;
DE   Flags: Precursor;
GN   Name=ELA1;
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   STRAIN=Holstein-Friesian; 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pancreas;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts upon elastin.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins, including elastin.
CC       Preferential cleavage: Ala-|-Xaa.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
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; M80838; AAA98525.1; -; mRNA.
DR   EMBL; BC149525; AAI49526.1; -; mRNA.
DR   IPI; IPI00688976; -.
DR   RefSeq; NP_776473.1; -.
DR   UniGene; Bt.4522; -.
DR   HSSP; P00772; 1QNJ.
DR   SMR; Q28153; 27-266.
DR   MEROPS; S01.153; -.
DR   Ensembl; ENSBTAG00000008900; Bos taurus.
DR   GeneID; 281139; -.
DR   KEGG; bta:281139; -.
DR   HOVERGEN; Q28153; -.
DR   OMA; Q28153; GSWHHTC.
DR   BRENDA; 3.4.21.36; 251.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
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   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     16       By similarity.
FT   PROPEP       17     26       Activation peptide (By similarity).
FT                                /FTId=PRO_0000027671.
FT   CHAIN        27    266       Elastase-1.
FT                                /FTId=PRO_0000027672.
FT   DOMAIN       27    264       Peptidase S1.
FT   ACT_SITE     71     71       Charge relay system (By similarity).
FT   ACT_SITE    119    119       Charge relay system (By similarity).
FT   ACT_SITE    214    214       Charge relay system (By similarity).
FT   METAL        85     85       Calcium (By similarity).
FT   METAL        90     90       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        95     95       Calcium (By similarity).
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    241    241       N-linked (GlcNAc...) (Potential).
FT   DISULFID     56     72       By similarity.
FT   DISULFID    153    220       By similarity.
FT   DISULFID    184    200       By similarity.
FT   DISULFID    210    240       By similarity.
SQ   SEQUENCE   266 AA;  28518 MW;  927E29C69BAF67E7 CRC64;
     MLRLLVFTSL VLYGHSTQDF PETNARVVGG TAVSKNSWPS QISLQYKSGS SWYHTCGGTL
     IKQKWVMTAA HCVDSQMTFR VVLGDHNLSQ NDGTEQYISV QKIVVHPSWN SNNVAAGYDI
     AVLRLAQSAT LNSYVQLGVL PQSGTILANN TPCYITGWGR TKTNGQLAQT LQQAYLPSVD
     YATCSSSSYW GSTVKTTMVC AGGDGVRAGC QGDSGGPLHC LVNGQYAVHG VTSFVSSLGC
     NVSKKPTVFT RVSAYISWIN NAIASN
//