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P00774 (CEL2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsin-like elastase family member 2A

EC=3.4.21.71
Alternative name(s):
Elastase-2
Elastase-2A
Gene names
Name:Cela2a
Synonyms:Ela2, Ela2a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 3014Activation peptide
PRO_0000027691
Chain31 – 271241Chymotrypsin-like elastase family member 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

Sequences

Sequence LengthMass (Da)Tools
P00774 [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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01233 mRNA. Translation: CAA24543.1.
L00124 expand/collapse EMBL AC list , L00118, L00119, L00120, L00121, L00122, L00123 Genomic DNA. Translation: AAA98780.1.
PIRELRT2. A00961.
RefSeqNP_036685.1. NM_012553.2.
UniGeneRn.10272.

3D structure databases

ProteinModelPortalP00774.
SMRP00774. Positions 31-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000018349.

Chemistry

BindingDBP00774.
ChEMBLCHEMBL3888.

Protein family/group databases

MEROPSS01.155.

PTM databases

PhosphoSiteP00774.

Proteomic databases

PaxDbP00774.
PRIDEP00774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018349; ENSRNOP00000018349; ENSRNOG00000013628.
GeneID24332.
KEGGrno:24332.
UCSCRGD:2548. rat.

Organism-specific databases

CTD63036.
RGD2548. Cela2a.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00640000091262.
HOGENOMHOG000251820.
InParanoidP00774.
KOK01346.
OMAASNGQWQ.
OrthoDBEOG75B84T.
PhylomeDBP00774.
TreeFamTF330455.

Gene expression databases

GenevestigatorP00774.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603011.
PROP00774.

Entry information

Entry nameCEL2A_RAT
AccessionPrimary (citable) accession number: P00774
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries