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Reviewed, UniProtKB/Swiss-Prot P08419 (ELA2A_PIG)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Elastase-2A
    EC=3.4.21.71
Alternative name(s):
    Elastase-2
Gene names
Name: ELA2A
Synonyms: ELA2
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts upon elastin.

Catalytic activity

Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.

Subcellular location

Secreted.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 2812Activation peptide
PRO_0000027689
Chain29 – 269241Elastase-2A
PRO_0000027690

Regions

Domain29 – 267239Peptidase S1

Sites

Active site731Charge relay system
Active site1211Charge relay system
Active site2161Charge relay system

Amino acid modifications

Disulfide bond58 ↔ 74
Disulfide bond155 ↔ 222
Disulfide bond186 ↔ 202
Disulfide bond212 ↔ 243

Experimental info

Sequence conflict101L → S in BAA00166. Ref.2
Sequence conflict1181N → K in BAA00166. Ref.2
Sequence conflict1321S → Y in BAA00166. Ref.2
Sequence conflict1721I → V in BAA00166. Ref.2
Sequence conflict2021C → V in BAA00166. Ref.2

Secondary structure

1 ........................................... 269
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P08419-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: BAC6FE69AF4DDE56

FASTA26928,699
        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

« Hide

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References

[1]"Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas."
Kawashima I., Tani T., Shimoda K., Takiguchi Y.
DNA 6:163-172(1987) [PubMed: 3646943] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and expression in Escherichia coli of a cDNA encoding human pancreatic elastase 2."
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.
J. Biochem. 102:1555-1563(1987) [PubMed: 2834346] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

M16651 mRNA. Translation: AAA31027.1.
D00237 mRNA. Translation: BAA00166.1.
PIRA26823.
RefSeqNP_999274.1.
UniGeneSsc.316

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BRUX-ray2.30P29-269[»]
ModBaseSearch...

Protein family/group databases

MEROPSS01.155.

Genome annotation databases

GeneID397197.
KEGGssc:397197.

Phylogenomic databases

HOVERGENP08419.

Enzyme and pathway databases

BRENDA3.4.21.71. 249.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameELA2A_PIG
AccessionPrimary (citable) accession number: P08419
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents