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Q867B0 (CELA1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. 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, ELS1
OrganismCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length258 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 By similarity.

Catalytic activity

Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-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 – 88 By similarity
Propeptide9 – 1810Activation peptide
PRO_0000027673
Chain19 – 258240Chymotrypsin-like elastase family member 1
PRO_0000027674

Regions

Domain19 – 256238Peptidase S1

Sites

Active site631Charge relay system By similarity
Active site1111Charge relay system By similarity
Active site2061Charge relay system By similarity
Metal binding771Calcium By similarity
Metal binding821Calcium; via carbonyl oxygen By similarity
Metal binding871Calcium By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 64 By similarity
Disulfide bond145 ↔ 212 By similarity
Disulfide bond176 ↔ 192 By similarity
Disulfide bond202 ↔ 232 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q867B0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EA7FF7CB67F1C74F

FASTA25827,900
        10         20         30         40         50         60 
MLVLYGHSTQ DVPETNARVV GGTEARRNSW PSQISLQYLS GGKWYHTCGG TLIRQNWVMT 

        70         80         90        100        110        120 
AAHCVDRTMT FRVVIGEHNL SQNDGTEQSA SVQKIVVHPY WNSNDVSAGY DIALLRLAQK 

       130        140        150        160        170        180 
VTLNSYVQLG VLPQEGAILA NNSPCYITGW GLTKTNGQLA QVLQQAYLPT VDYAICSSSS 

       190        200        210        220        230        240 
YWGSIVKKSM VCAGGDGIRS GCQGDSGGPL HCSVNGKYTV HGVTSFVSSL GCNVSRKPTV 

       250 
FTRVSAYITW INNVIASN 

« Hide

References

[1]"Canis familiaris pancreatic elastase 1 mRNA, complete cds."
Kano R., Hasegawa A.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB100595 mRNA. Translation: BAC55894.1.
RefSeqNP_001003007.1. NM_001003007.1.
UniGeneCfa.12.

3D structure databases

ProteinModelPortalQ867B0.
SMRQ867B0. Positions 19-258.
ModBaseSearch...

Protein family/group databases

MEROPSS01.153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403515.
KEGGcfa:403515.

Organism-specific databases

CTD1990.

Phylogenomic databases

eggNOGmaNOG15434.
GeneTreeENSGT00550000074117.
InParanoidQ867B0.
OrthoDBEOG4V171P.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
KOK01326.
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCELA1_CANFA
AccessionPrimary (citable) accession number: Q867B0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families