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Reviewed, UniProtKB/Swiss-Prot Q28153 (ELA1_BOVIN)

Last modified June 16, 2009. Version 70. 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

Names and origin

Protein namesRecommended name:
    Elastase-1
    EC=3.4.21.36
Alternative name(s):
    Elastase I
Gene names
Name: ELA1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length266 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

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.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium 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 – 1616 By similarity
Propeptide17 – 2610Activation peptide By similarity
PRO_0000027671
Chain27 – 266240Elastase-1
PRO_0000027672

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

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 72 By similarity
Disulfide bond153 ↔ 220 By similarity
Disulfide bond184 ↔ 200 By similarity
Disulfide bond210 ↔ 240 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28153-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 927E29C69BAF67E7

FASTA26628,518
        10         20         30         40         50         60 
MLRLLVFTSL VLYGHSTQDF PETNARVVGG TAVSKNSWPS QISLQYKSGS SWYHTCGGTL 

        70         80         90        100        110        120 
IKQKWVMTAA HCVDSQMTFR VVLGDHNLSQ NDGTEQYISV QKIVVHPSWN SNNVAAGYDI 

       130        140        150        160        170        180 
AVLRLAQSAT LNSYVQLGVL PQSGTILANN TPCYITGWGR TKTNGQLAQT LQQAYLPSVD 

       190        200        210        220        230        240 
YATCSSSSYW GSTVKTTMVC AGGDGVRAGC QGDSGGPLHC LVNGQYAVHG VTSFVSSLGC 

       250        260 
NVSKKPTVFT RVSAYISWIN NAIASN 

« Hide

References

« Hide 'large scale' references
[1]"Bovine pancreatic preproelastases I and II: comparison of nucleotide and amino acid sequences and tissue specific expression."
Gestin M., le Huerou-Luron I., Wicker-Planquart C., le Drean G., Chaix J.-C., Puigserver A., Guilloteau P.
Comp. Biochem. Physiol. 118B:181-187(1997) [PubMed: 9418008] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Holstein-Friesian.
Tissue: Pancreas.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pancreas.

Cross-references

Sequence databases

M80838 mRNA. Translation: AAA98525.1.
BC149525 mRNA. Translation: AAI49526.1.
IPIIPI00688976.
RefSeqNP_776473.1.
UniGeneBt.4522

3D structure databases

HSSPHSSP built from PDB template 1QNJ based on UniProtKB P00772.
SMRQ28153. Positions 27-266.
ModBaseSearch...

Protein family/group databases

MEROPSS01.153.

Genome annotation databases

EnsemblENSBTAG00000008900. Bos taurus. [Contig view]
GeneID281139.
KEGGbta:281139.

Phylogenomic databases

HOVERGENQ28153.
OMAQ28153. GSWHHTC.

Enzyme and pathway databases

BRENDA3.4.21.36. 251.

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...

Entry information

Entry nameELA1_BOVIN
AccessionPrimary (citable) accession number: Q28153
Secondary accession number(s): A6QPW5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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