[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00535a053; PubMed=6918221 [NCBI, ExPASy, EBI, Israel, Japan] MacDonald R.J., Swift G.H., Quinto C., Swain W., Pictet R.L., Nikovits W., Rutter W.J.; "Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences."; Biochemistry 21:1453-1463(1982).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6094548 [NCBI, ExPASy, EBI, Israel, Japan] Swift G.H., Craik C.S., Stary S.J., Quinto C., Lahaie R.G., Rutter W.J., MacDonald R.J.; "Structure of the two related elastase genes expressed in the rat pancreas."; J. Biol. Chem. 259:14271-14278(1984).

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

V01233; CAA24543.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00124; AAA98780.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00118; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00119; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00120; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00121; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00122; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00123; AAA98780.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A00961; ELRT2.

NP_036685.1; -.

3D structure databases

HSSP

P08419; 1BRU. [HSSP ENTRY / PDB]

SMR

P00774; 31-271.

ModBase

P00774.

Protein family/group databases

MEROPS

S01.155; -.

Organism-specific databases

RGD

2548; Ela2a.

Gene expression databases

ArrayExpress

P00774; -.

GermOnline

ENSRNOG00000013628; Rattus norvegicus.

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

Ensembl

ENSRNOG00000013628; Rattus norvegicus. [Contig view]

GeneID

24332; -.

KEGG

rno:24332; -.

Phylogenomic databases

HOVERGEN

P00774; -.

Other

NextBio

603011; -.

UniRef

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

Keywords

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 30`	`14`	`Activation peptide.`	`PRO_0000027691`
`CHAIN`	`31 271`	`241`	`Elastase-2A.`	`PRO_0000027692`
`DOMAIN`	`31 269`	`239`	`Peptidase S1.`
`ACT_SITE`	`75 75`		`Charge relay system (By similarity).`
`ACT_SITE`	`123 123`		`Charge relay system (By similarity).`
`ACT_SITE`	`218 218`		`Charge relay system (By similarity).`
`DISULFID`	`60 76`		`By similarity.`
`DISULFID`	`157 224`		`By similarity.`
`DISULFID`	`188 204`		`By similarity.`
`DISULFID`	`214 245`		`By similarity.`

Sequence information

Length: 271 AA [This is the length of the unprocessed precursor]

Molecular weight: 28885 Da [This is the MW of the unprocessed precursor]

CRC64: 125C783B857B71E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIRTLLLSAL VAGALSCGYP TYEVQHDVSR VVGGQEASPN SWPWQVSLQY LSSGKWHHTC 

        70         80         90        100        110        120 
GGSLVANNWV LTAAHCISNS RTYRVLLGRH SLSTSESGSL AVQVSKLVVH EKWNAQKLSN 

       130        140        150        160        170        180 
GNDIALVKLA SPVALTSKIQ TACLPPAGTI LPNNYPCYVT GWGRLQTNGA TPDVLQQGRL 

       190        200        210        220        230        240 
LVVDYATCSS ASWWGSSVKT NMVCAGGDGV TSSCNGDSGG PLNCQASNGQ WQVHGIVSFG 

       250        260        270 
STLGCNYPRK PSVFTRVSNY IDWINSVIAK N

P00774 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