[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3646943 [NCBI, ExPASy, EBI, Israel, Japan] Kawashima I., Tani T., Shimoda K., Takiguchi Y.; "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas."; DNA 6:163-172(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2834346 [NCBI, ExPASy, EBI, Israel, Japan] Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y., Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y., Tanaka J., Ikenaga H.; "Molecular cloning and expression in Escherichia coli of a cDNA encoding human pancreatic elastase 2."; J. Biochem. 102:1555-1563(1987).

Comments

FUNCTION: Acts upon elastin.
CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.
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

Sequence databases

EMBL

M16651; AAA31027.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00237; BAA00166.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A26823; A26823.

NP_999274.1; -.

3D structure databases

PDB

1BRU; X-ray; 2.30 A; P=29-269.

[ExPASy / RCSB / EBI]

PDBsum

1BRU; -.

ModBase

P08419.

Protein family/group databases

MEROPS

S01.155; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (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).

Genome annotation databases

GeneID

397197; -.

KEGG

ssc:397197; -.

Phylogenomic databases

HOVERGEN

P08419; -.

Other

UniRef

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

Keywords

3D-structure; Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`
`PROPEP`	`17 28`	`12`	`Activation peptide.`	`PRO_0000027689`
`CHAIN`	`29 269`	`241`	`Elastase-2A.`	`PRO_0000027690`
`DOMAIN`	`29 267`	`239`	`Peptidase S1.`
`ACT_SITE`	`73 73`		`Charge relay system.`
`ACT_SITE`	`121 121`		`Charge relay system.`
`ACT_SITE`	`216 216`		`Charge relay system.`
`DISULFID`	`58 74`
`DISULFID`	`155 222`
`DISULFID`	`186 202`
`DISULFID`	`212 243`
`CONFLICT`	`10 10`		`L -> S (in Ref. 2; BAA00166).`
`CONFLICT`	`118 118`		`N -> K (in Ref. 2; BAA00166).`
`CONFLICT`	`132 132`		`S -> Y (in Ref. 2; BAA00166).`
`CONFLICT`	`172 172`		`I -> V (in Ref. 2; BAA00166).`
`CONFLICT`	`202 202`		`C -> V (in Ref. 2; BAA00166).`
`STRAND`	`43 50`	`8`
`STRAND`	`53 64`	`12`
`STRAND`	`67 70`	`4`
`HELIX`	`72 74`	`3`
`STRAND`	`81 86`	`6`
`STRAND`	`88 92`	`5`
`STRAND`	`98 107`	`10`
`HELIX`	`116 118`	`3`
`STRAND`	`123 129`	`7`
`STRAND`	`154 160`	`7`
`STRAND`	`174 181`	`8`
`HELIX`	`183 186`	`4`
`TURN`	`189 192`	`4`
`HELIX`	`193 195`	`3`
`STRAND`	`200 203`	`4`
`STRAND`	`206 210`	`5`
`STRAND`	`219 223`	`5`
`STRAND`	`229 237`	`9`
`STRAND`	`242 244`	`3`
`STRAND`	`250 254`	`5`
`HELIX`	`255 257`	`3`
`HELIX`	`259 268`	`10`

Sequence information

Length: 269 AA [This is the length of the unprocessed precursor]

Molecular weight: 28699 Da [This is the MW of the unprocessed precursor]

CRC64: BAC6FE69AF4DDE56 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIRALLLSTL VAGALSCGLP ANLPQLPRVV GGEDARPNSW PWQVSLQYDS SGQWRHTCGG 

        70         80         90        100        110        120 
TLVDQSWVLT AAHCISSSRT YRVVLGRHSL STNEPGSLAV KVSKLVVHQD WNSNQLSNGN 

       130        140        150        160        170        180 
DIALLKLASP VSLTDKIQLG CLPAAGTILP NNYVCYVTGW GRLQTNGASP DILQQGQLLV 

       190        200        210        220        230        240 
VDYATCSKPG WWGSTVKTNM ICAGGDGIIS SCNGDSGGPL NCQGANGQWQ VHGIVSFGSS 

       250        260 
LGCNYYHKPS VFTRVSNYID WINSVIANN

P08419 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