[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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).
[3]	PROTEIN SEQUENCE OF 17-45. TISSUE=Pancreas; DOI=10.1021/bi00285a008; PubMed=6555050 [NCBI, ExPASy, EBI, Israel, Japan] Largman C.; "Isolation and characterization of rat pancreatic elastase."; Biochemistry 22:3763-3770(1983).

Comments

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

V01234; CAA24544.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00117; AAA98811.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00112; AAA98811.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00113; AAA98811.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00114; AAA98811.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00115; AAA98811.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00116; AAA98811.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A00960; ELRT1.

UniGene

Rn.6044

3D structure databases

HSSP

P00772; 1QNJ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P00773; 27-264.

ModBase

P00773.

Protein family/group databases

MEROPS

S01.153; -.

Organism-specific databases

RGD

2547; Ela1.

Gene expression databases

ArrayExpress

P00773; -.

GermOnline

ENSRNOG00000004725; Rattus norvegicus.

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).

Genome annotation databases

Ensembl

ENSRNOG00000004725; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P00773; -.

Other

UniRef

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

Keywords

Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`
`PROPEP`	`17 26`	`10`	`Activation peptide.`	`PRO_0000027683`
`CHAIN`	`27 266`	`240`	`Elastase-1.`	`PRO_0000027684`
`DOMAIN`	`27 264`	`238`	`Peptidase S1.`
`ACT_SITE`	`71 71`		`Charge relay system (By similarity).`
`ACT_SITE`	`119 119`		`Charge relay system (By similarity).`
`ACT_SITE`	`214 214`		`Charge relay system (By similarity).`
`METAL`	`85 85`		`Calcium (By similarity).`
`METAL`	`90 90`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`95 95`		`Calcium (By similarity).`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`153 220`		`By similarity.`
`DISULFID`	`184 200`		`By similarity.`
`DISULFID`	`210 240`		`By similarity.`
`CONFLICT`	`104 104`		`M -> V (in Ref. 2; AAA98811).`
`CONFLICT`	`108 108`		`T -> N (in Ref. 2; AAA98811).`
`CONFLICT`	`244 244`		`K -> R (in Ref. 2; AAA98811).`
`CONFLICT`	`266 266`		`T -> N (in Ref. 2; AAA98811).`

Sequence information

Length: 266 AA [This is the length of the unprocessed precursor]

Molecular weight: 28976 Da [This is the MW of the unprocessed precursor]

CRC64: 5A56FE8FCF1AAEDA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRFLVFASL VLYGHSTQDF PETNARVVGG AEARRNSWPS QISLQYLSGG SWYHTCGGTL 

        70         80         90        100        110        120 
IRRNWVMTAA HCVSSQMTFR VVVGDHNLSQ NDGTEQYVSV QKIMVHPTWN SNNVAAGYDI 

       130        140        150        160        170        180 
ALLRLAQSVT LNNYVQLAVL PQEGTILANN NPCYITGWGR TRTNGQLSQT LQQAYLPSVD 

       190        200        210        220        230        240 
YSICSSSSYW GSTVKTTMVC AGGDGVRSGC QGDSGGPLHC LVNGQYSVHG VTSFVSSMGC 

       250        260 
NVSKKPTVFT RVSAYISWMN NVIAYT

P00773 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