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P00772 (CELA1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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.

Subcellular location

Secreted.

Tissue specificity

Pancreas. Basal layers of the epidermis, hair follicle and sebaceous gland epithelia (at protein level). Ref.5

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
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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

protein binding

Inferred from physical interaction. Source: IntAct

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SERPINA1P010092EBI-986248,EBI-986224From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 2610Activation peptide
PRO_0000027681
Chain27 – 266240Chymotrypsin-like elastase family member 1
PRO_0000027682

Regions

Domain27 – 264238Peptidase S1

Sites

Active site711Charge relay system Ref.3 Ref.7
Active site1191Charge relay system Ref.7
Active site2141Charge relay system Ref.7
Metal binding851Calcium
Metal binding901Calcium; via carbonyl oxygen
Metal binding951Calcium

Amino acid modifications

Disulfide bond56 ↔ 72 Ref.3
Disulfide bond153 ↔ 220
Disulfide bond184 ↔ 200
Disulfide bond210 ↔ 240

Experimental info

Sequence conflict921D → N AA sequence Ref.3
Sequence conflict1261A → G in BAA00118. Ref.2
Sequence conflict1841C → L in BAA00118. Ref.2
Sequence conflict2041D → N AA sequence Ref.3

Secondary structure

1 ........................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00772 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: BF07D6855BB50FE2

FASTA26628,821
        10         20         30         40         50         60 
MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS SWAHTCGGTL 

        70         80         90        100        110        120 
IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV QKIVVHPYWN TDDVAAGYDI 

       130        140        150        160        170        180 
ALLRLAQSVT LNSYVQLGVL PRAGTILANN SPCYITGWGL TRTNGQLAQT LQQAYLPTVD 

       190        200        210        220        230        240 
YAICSSSSYW GSTVKNSMVC AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC 

       250        260 
NVTRKPTVFT RVSAYISWIN NVIASN

« Hide

References

[1]"Isolation and expression in Escherichia coli of a cDNA clone encoding porcine pancreatic elastase."
Shirasu Y., Yoshida H., Mikayama T., Matsuki S., Tanaka J., Ikenaga H.
J. Biochem. 99:1707-1712(1986) [PubMed: 3528137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region."
Tani T., Kawashima I., Furukawa H., Ohmine T., Takiguchi Y.
J. Biochem. 101:591-599(1987) [PubMed: 3648024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Evidence for the amino acid sequence of porcine pancreatic elastase."
Shotton D.M., Hartley B.S.
Biochem. J. 131:643-675(1973) [PubMed: 4578945] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-266.
[4]"Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases."
Shotton D.M., Hartley B.S.
Nature 225:802-806(1970) [PubMed: 5415108] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-266.
[5]"Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism."
Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.
J. Invest. Dermatol. 114:165-170(2000) [PubMed: 10620133] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"The atomic structure of crystalline porcine pancreatic elastase at 2.5-A resolution: comparisons with the structure of alpha-chymotrypsin."
Sawyer L., Shotton D.M., Campbell J.W., Wendell P.L., Muirhead H., Watson H.C., Diamond R., Ladner R.C.
J. Mol. Biol. 118:137-208(1978) [PubMed: 628010] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]"Three-dimensional structure of tosyl-elastase."
Shotton D.M., Watson H.C.
Nature 225:811-816(1970) [PubMed: 5415110] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), ACTIVE SITE.
[8]"The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase."
Huang K., Strynadka N.C., Bernard V.D., Peanasky R.J., James M.N.
Structure 2:679-689(1994) [PubMed: 7922044] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04036 Transcribed RNA. Translation: CAA27670.1.
D00160 mRNA. Translation: BAA00118.1.
PIRELPG. JS0013.
RefSeqNP_998988.1. NM_213823.1.
UniGeneSsc.89635.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
4ESTX-ray1.78E27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortalP00772.
SMRP00772. Positions 27-266.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-378N.
IntActP00772. 1 interaction.

Protein family/group databases

MEROPSS01.153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000000239; ENSSSCP00000000235; ENSSSCG00000000222.
GeneID396766.
KEGGssc:396766.

Organism-specific databases

CTD1990.

Phylogenomic databases

GeneTreeENSGT00550000074117.
OMAPSVDYAT.
OrthoDBEOG4V171P.

Enzyme and pathway databases

BRENDA3.4.21.36. 6170.

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_PIG
AccessionPrimary (citable) accession number: P00772
Secondary accession number(s): Q29625
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 16, 2011
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents