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P00773 (CELA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. 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 1

EC=3.4.21.36
Alternative name(s):
Elastase-1
Gene names
Name:Cela1
Synonyms:Ela1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.3
Propeptide17 – 2610Activation peptide
PRO_0000027683
Chain27 – 266240Chymotrypsin-like elastase family member 1
PRO_0000027684

Regions

Domain27 – 264238Peptidase S1

Sites

Active site711Charge relay system By similarity
Active site1191Charge relay system By similarity
Active site2141Charge relay system By similarity
Metal binding851Calcium By similarity
Metal binding901Calcium; via carbonyl oxygen By similarity
Metal binding951Calcium By similarity

Amino acid modifications

Disulfide bond56 ↔ 72 By similarity
Disulfide bond153 ↔ 220 By similarity
Disulfide bond184 ↔ 200 By similarity
Disulfide bond210 ↔ 240 By similarity

Experimental info

Sequence conflict1041M → V in AAA98811. Ref.2
Sequence conflict1081T → N in AAA98811. Ref.2
Sequence conflict2441K → R in AAA98811. Ref.2
Sequence conflict2661T → N in AAA98811. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00773 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5A56FE8FCF1AAEDA

FASTA26628,976
        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 

« 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 [GENOMIC DNA].
[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].
[3]"Isolation and characterization of rat pancreatic elastase."
Largman C.
Biochemistry 22:3763-3770(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-45.
Tissue: Pancreas.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01234 mRNA. Translation: CAA24544.1.
L00117 expand/collapse EMBL AC list , L00112, L00113, L00114, L00115, L00116 Genomic DNA. Translation: AAA98811.1.
PIRELRT1. A00960.
RefSeqNP_036684.1. NM_012552.3.
UniGeneRn.6044.

3D structure databases

ProteinModelPortalP00773.
SMRP00773. Positions 27-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000006351.

Protein family/group databases

MEROPSS01.153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006351; ENSRNOP00000006351; ENSRNOG00000004725.
GeneID24331.
KEGGrno:24331.
UCSCRGD:2547. rat.

Organism-specific databases

CTD1990.
RGD2547. Cela1.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00640000091262.
HOGENOMHOG000251820.
InParanoidP00773.
KOK01326.
OrthoDBEOG7RRF7Z.
PhylomeDBP00773.
TreeFamTF330455.

Gene expression databases

GenevestigatorP00773.

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

NextBio603007.
PROP00773.

Entry information

Entry nameCELA1_RAT
AccessionPrimary (citable) accession number: P00773
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 115 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