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Reviewed, UniProtKB/Swiss-Prot P09582 (ESTA_CANFA)

Last modified May 26, 2009. Version 77. 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:
    Arginine esterase
    EC=3.4.21.35
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This serine protease is found in dog seminal plasma, its exact physiological function is not known.

Catalytic activity

Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.

Induction

By androgens.

Sequence similarities

Belongs to the peptidase S1 family. Kallikrein subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   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 – 1717 Potential
Propeptide18 – 247Activation peptide Ref.3
PRO_0000028019
Chain25 – 260236Arginine esterase
PRO_0000028020

Regions

Domain25 – 257233Peptidase S1

Sites

Active site651Charge relay system By similarity
Active site1191Charge relay system By similarity
Active site2121Charge relay system By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Probable
Disulfide bond31 ↔ 172 By similarity
Disulfide bond50 ↔ 66 By similarity
Disulfide bond151 ↔ 218 By similarity
Disulfide bond183 ↔ 197 By similarity
Disulfide bond208 ↔ 233 By similarity

Experimental info

Sequence conflict561N → H in AAA30831. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P09582-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 48768B6EF204775A

FASTA26028,746
        10         20         30         40         50         60 
MWFLALCLAM SLGWTGAEPH FQPRIIGGRE CLKNSQPWQV AVYHNGEFAC GGVLVNPEWV 

        70         80         90        100        110        120 
LTAAHCANSN CEVWLGRHNL SESEDEGQLV QVRKSFIHPL YKTKVPRAVI RPGEDRSHDL 

       130        140        150        160        170        180 
MLLHLEEPAK ITKAVRVMDL PKKEPPLGST CYVSGWGSTD PETIFHPGSL QCVDLKLLSN 

       190        200        210        220        230        240 
NQCAKVYTQK VTKFMLCAGV LEGKKDTCKG DSGGPLICDG ELVGITSWGA TPCGKPQMPS 

       250        260 
LYTRVMPHLM WIKDTMKANT 

« Hide

References

[1]"Nucleotide sequence of the androgen-dependent arginine esterase mRNA of canine prostate."
Chapdelaine P., Ho-Kim M.-A., Tremblay R.R., Dube J.Y.
FEBS Lett. 232:187-192(1988) [PubMed: 2835268] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.
[2]"Characterization and expression of the prostatic arginine esterase gene, a canine glandular kallikrein."
Chapdelaine P., Gauthier E., Ho-Kim M.-A., Bissonnette L., Tremblay R.R., Dube J.Y.
DNA Cell Biol. 10:49-59(1991) [PubMed: 1991049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The major androgen-dependent protease in dog prostate belongs to the kallikrein family: confirmation by partial amino acid sequencing."
Lazure C., Leduc R., Seidah N.G., Chretien M., Dube J.Y., Chapdelaine P., Frenette G., Paquin R., Tremblay R.R.
FEBS Lett. 175:1-7(1984) [PubMed: 6566614] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-50 AND 108-145.
Tissue: Prostate.
[4]"Androgen regulation of canine prostatic arginine esterase mRNA using cloned cDNA."
Chapdelaine P., Potvin C., Ho-Kim M.A., Larouche L., Bellemare G., Tremblay R.T., Dube J.Y.
Mol. Cell. Endocrinol. 56:63-70(1988) [PubMed: 3371547] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 105-260.

Cross-references

Sequence databases

Y00751 mRNA. Translation: CAA68720.1.
M63669 Genomic DNA. Translation: AAA30831.1.
PIRA30981.
A37938.
RefSeqNP_001003284.1.
UniGeneCfa.3836

3D structure databases

HSSPHSSP built from PDB template 2PKA based on UniProtKB P00752.
ModBaseSearch...

Protein family/group databases

MEROPSS01.289.

Genome annotation databases

GeneID403967.
KEGGcfa:403967.

Phylogenomic databases

HOVERGENP09582.

Enzyme and pathway databases

BRENDA3.4.21.35. 463.

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 nameESTA_CANFA
AccessionPrimary (citable) accession number: P09582
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 26, 2009
This is version 77 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