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Reviewed, UniProtKB/Swiss-Prot P00774 (ELA2A_RAT)

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

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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
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 – 3014Activation peptide
PRO_0000027691
Chain31 – 271241Elastase-2A
PRO_0000027692

Regions

Domain31 – 269239Peptidase S1

Sites

Active site751Charge relay system By similarity
Active site1231Charge relay system By similarity
Active site2181Charge relay system By similarity

Amino acid modifications

Disulfide bond60 ↔ 76 By similarity
Disulfide bond157 ↔ 224 By similarity
Disulfide bond188 ↔ 204 By similarity
Disulfide bond214 ↔ 245 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P00774-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 125C783B857B71E3

FASTA27128,885
        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

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References

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

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Cross-references

Sequence databases

V01233 mRNA. Translation: CAA24543.1.
L00124 expand/collapse EMBL AC list , L00118, L00119, L00120, L00121, L00122, L00123 Genomic DNA. Translation: AAA98780.1.
IPIIPI00212792.
PIRELRT2. A00961.
RefSeqNP_036685.1.
UniGeneRn.10272

3D structure databases

HSSPHSSP built from PDB template 1BRU based on UniProtKB P08419.
SMRP00774. Positions 31-271.
ModBaseSearch...

Protein family/group databases

MEROPSS01.155.

Genome annotation databases

EnsemblENSRNOG00000013628. Rattus norvegicus. [Contig view]
GeneID24332.
KEGGrno:24332.

Organism-specific databases

RGD2548. Ela2a.

Phylogenomic databases

HOVERGENP00774.

Enzyme and pathway databases

BRENDA3.4.21.71. 248.

Gene expression databases

ArrayExpressP00774.
GermOnlineENSRNOG00000013628. Rattus norvegicus.

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...

Other Resources

NextBio603011.

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Entry information

Entry nameELA2A_RAT
AccessionPrimary (citable) accession number: P00774
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
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

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