[1]	FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. PubMed=9628006 [NCBI, ExPASy, EBI, Israel, Japan] Berglund G.I., Smalaas A.O., Outzen H., Willassen N.P.; "Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar)."; Mol. Mar. Biol. Biotechnol. 7:105-114(1998).
[2]	CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). DOI=10.1107/S0907444994011066; PubMed=15299308 [NCBI, ExPASy, EBI, Israel, Japan] Berglund G.I., Smalaas A.O., Hansen L.K., Willassen N.P.; "Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar)."; Acta Crystallogr. D 51:393-394(1995).
[3]	X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), COFACTOR, AND DISULFIDE BONDS. DOI=10.1107/S0907444995004835; PubMed=15299762 [NCBI, ExPASy, EBI, Israel, Japan] Berglund G.I., Willassen N.P., Hordvik A., Smalaas A.O.; "Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution."; Acta Crystallogr. D 51:925-937(1995).

Comments

FUNCTION: Acts upon elastin.
CATALYTIC ACTIVITY: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
COFACTOR: Binds 1 calcium ion per subunit.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=1.47 mM for Suc-AAA-pNA (at 22 degrees Celsius);
	K_M=1.34 mM for Suc-AAPL-pNA (at 22 degrees Celsius);
	K_M=0.82 mM for Suc-AAPV-pNA (at 22 degrees Celsius);
	K_M=0.83 mM for Suc-AAPA-pNA (at 22 degrees Celsius);
	K_M=0.15 mM for Suc-AAPI-pNA (at 22 degrees Celsius);
pH dependence:	Optimum pH is 8.1 at 22 degrees Celsius with Suc-AAA-pNA as the substrate;

SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Pancreas.
SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

1ELT; X-ray; 1.61 A; A=1-236.

[ExPASy / RCSB / EBI]

PDBsum

1ELT; -.

ModBase

Q7SIG3.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

Q7SIG3; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Hydrolase; Metal-binding; Protease; Secreted; Serine protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 236`	`236`	`Elastase-1.`	`PRO_0000248261`
`DOMAIN`	`1 236`	`236`	`Peptidase S1.`
`ACT_SITE`	`45 45`		`Charge relay system.`
`ACT_SITE`	`93 93`		`Charge relay system.`
`ACT_SITE`	`187 187`		`Charge relay system.`
`METAL`	`59 59`		`Calcium.`
`METAL`	`61 61`		`Calcium; via carbonyl oxygen.`
`METAL`	`64 64`		`Calcium; via carbonyl oxygen.`
`METAL`	`66 66`		`Calcium.`
`METAL`	`69 69`		`Calcium.`
`DISULFID`	`30 46`
`DISULFID`	`127 193`
`DISULFID`	`158 174`
`DISULFID`	`183 213`
`STRAND`	`2 6`	`5`
`STRAND`	`15 22`	`8`
`STRAND`	`25 36`	`12`
`STRAND`	`39 42`	`4`
`HELIX`	`44 47`	`4`
`STRAND`	`53 58`	`6`
`STRAND`	`70 72`	`3`
`STRAND`	`74 79`	`6`
`HELIX`	`88 90`	`3`
`STRAND`	`95 101`	`7`
`STRAND`	`106 108`	`3`
`STRAND`	`127 132`	`6`
`STRAND`	`146 149`	`4`
`HELIX`	`155 158`	`4`
`TURN`	`161 164`	`4`
`HELIX`	`165 167`	`3`
`STRAND`	`172 175`	`4`
`STRAND`	`190 195`	`6`
`STRAND`	`198 207`	`10`
`STRAND`	`220 224`	`5`
`HELIX`	`225 228`	`4`
`HELIX`	`229 235`	`7`

Sequence information

Length: 236 AA [This is the length of the unprocessed precursor]

Molecular weight: 25015 Da [This is the MW of the unprocessed precursor]

CRC64: 06CF7DB4E1397E97 [This is a checksum on the sequence]

        10         20         30         40         50         60 
VVGGRVAQPN SWPWQISLQY KSGSSYYHTC GGSLIRQGWV MTAAHCVDSA RTWRVVLGEH 

        70         80         90        100        110        120 
NLNTNEGKEQ IMTVNSVFIH SGWNSDDVAG GYDIALLRLN TQASLNSAVQ LAALPPSNQI 

       130        140        150        160        170        180 
LPNNNPCYIT GWGKTSTGGP LSDSLKQAWL PSVDHATCSS SGWWGSTVKT TMVCAGGGAN 

       190        200        210        220        230 
SGCNGDSGGP LNCQVNGSYY VHGVTSFVSS SGCNASKKPT VFTRVSAYIS WMNGIM

Q7SIG3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools