Reviewed, UniProtKB/Swiss-Prot Q7SIG3 (ELA1_SALSA)

Names and origin

Protein names	Recommended name:     Elastase-1     EC=3.4.21.36
Organism	Salmo salar (Atlantic salmon)
Taxonomic identifier	8030 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonidae › Salmoninae › Salmo

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts upon elastin. Ref.1
Catalytic activity	Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa. Ref.1
Cofactor	Binds 1 calcium ion per subunit. Ref.3
Subcellular location	Secreted. Ref.1
Tissue specificity	Pancreas. Ref.1
Sequence similarities	Belongs to the peptidase S1 family. Elastase subfamily. Contains 1 peptidase S1 domain.
biophysicochemical properties	Kinetic parameters: KM=1.47 mM for Suc-AAA-pNA (at 22 degrees Celsius) Ref.1 KM=1.34 mM for Suc-AAPL-pNA (at 22 degrees Celsius) Ref.1 KM=0.82 mM for Suc-AAPV-pNA (at 22 degrees Celsius) Ref.1 KM=0.83 mM for Suc-AAPA-pNA (at 22 degrees Celsius) Ref.1 KM=0.15 mM for Suc-AAPI-pNA (at 22 degrees Celsius) Ref.1 pH dependence: Optimum pH is 8.1 at 22 degrees Celsius with Suc-AAA-pNA as the substrate. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 236

236

Elastase-1

PRO_0000248261

Regions

Domain

1 – 236

236

Peptidase S1

Sites

Active site

45

1

Charge relay system Ref.3

Active site

93

1

Charge relay system Ref.3

Active site

187

1

Charge relay system Ref.3

Metal binding

59

1

Calcium Ref.3

Metal binding

61

1

Calcium; via carbonyl oxygen Ref.3

Metal binding

64

1

Calcium; via carbonyl oxygen Ref.3

Metal binding

66

1

Calcium Ref.3

Metal binding

69

1

Calcium Ref.3

Amino acid modifications

Disulfide bond

30 ↔ 46

Ref.3

Disulfide bond

127 ↔ 193

Ref.3

Disulfide bond

158 ↔ 174

Ref.3

Disulfide bond

183 ↔ 213

Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

236

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

15 – 22

8

Beta strand

25 – 36

12

Beta strand

39 – 42

4

Helix

44 – 47

4

Beta strand

53 – 58

6

Beta strand

70 – 72

3

Beta strand

74 – 79

6

Helix

88 – 90

3

Beta strand

95 – 101

7

Beta strand

106 – 108

3

Beta strand

127 – 132

6

Beta strand

146 – 149

4

Helix

155 – 158

4

Turn

161 – 164

4

Helix

165 – 167

3

Beta strand

172 – 175

4

Beta strand

190 – 195

6

Beta strand

198 – 207

10

Beta strand

220 – 224

5

Helix

225 – 228

4

Helix

229 – 235

7

Sequences

	Sequence		Length	Mass (Da)
	Q7SIG3-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 06CF7DB4E1397E97	FASTA	236	25,015
	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

References

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

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ELT	X-ray	1.61	A	1-236	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.153.

Phylogenomic databases

HOVERGEN

Q7SIG3.

Enzyme and pathway databases

BRENDA

3.4.21.36. 39345.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ELA1_SALSA

Accession

Primary (citable) accession number: Q7SIG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)