[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Prostate; DOI=10.1016/0014-5793(88)80414-9; PubMed=2835268 [NCBI, ExPASy, EBI, Israel, Japan] Chapdelaine P., Ho-Kim M.-A., Tremblay R.R., Dube J.Y.; "Nucleotide sequence of the androgen-dependent arginine esterase mRNA of canine prostate."; FEBS Lett. 232:187-192(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1991049 [NCBI, ExPASy, EBI, Israel, Japan] Chapdelaine P., Gauthier E., Ho-Kim M.-A., Bissonnette L., Tremblay R.R., Dube J.Y.; "Characterization and expression of the prostatic arginine esterase gene, a canine glandular kallikrein."; DNA Cell Biol. 10:49-59(1991).
[3]	PROTEIN SEQUENCE OF 25-50 AND 108-145. TISSUE=Prostate; DOI=10.1016/0014-5793(84)80557-8; PubMed=6566614 [NCBI, ExPASy, EBI, Israel, Japan] Lazure C., Leduc R., Seidah N.G., Chretien M., Dube J.Y., Chapdelaine P., Frenette G., Paquin R., Tremblay R.R.; "The major androgen-dependent protease in dog prostate belongs to the kallikrein family: confirmation by partial amino acid sequencing."; FEBS Lett. 175:1-7(1984).
[4]	NUCLEOTIDE SEQUENCE OF 105-260. DOI=10.1016/0303-7207(88)90009-3; PubMed=3371547 [NCBI, ExPASy, EBI, Israel, Japan] Chapdelaine P., Potvin C., Ho-Kim M.A., Larouche L., Bellemare G., Tremblay R.T., Dube J.Y.; "Androgen regulation of canine prostatic arginine esterase mRNA using cloned cDNA."; Mol. Cell. Endocrinol. 56:63-70(1988).

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.
SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00751; CAA68720.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63669; AAA30831.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A30981; A30981.
A37938; A37938.

RefSeq

NP_001003284.1; -.

UniGene

Cfa.3836

3D structure databases

HSSP

P00752; 2PKA. [HSSP ENTRY / PDB]

ModBase

P09582.

Protein family/group databases

MEROPS

S01.289; -.

Ontologies

GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

403967; -.

KEGG

cfa:403967; -.

Phylogenomic databases

HOVERGEN

P09582; -.

Other

ProtoNet

P09582.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 24`	`7`	`Activation peptide.`	`PRO_0000028019`
`CHAIN`	`25 260`	`236`	`Arginine esterase.`	`PRO_0000028020`
`DOMAIN`	`25 257`	`233`	`Peptidase S1.`
`ACT_SITE`	`65 65`		`Charge relay system (By similarity).`
`ACT_SITE`	`119 119`		`Charge relay system (By similarity).`
`ACT_SITE`	`212 212`		`Charge relay system (By similarity).`
`CARBOHYD`	`79 79`		`N-linked (GlcNAc...) (Probable).`
`DISULFID`	`31 172`		`By similarity.`
`DISULFID`	`50 66`		`By similarity.`
`DISULFID`	`151 218`		`By similarity.`
`DISULFID`	`183 197`		`By similarity.`
`DISULFID`	`208 233`		`By similarity.`
`CONFLICT`	`56 56`		`N -> H (in Ref. 2; AAA30831).`

Sequence information

Length: 260 AA [This is the length of the unprocessed precursor]

Molecular weight: 28746 Da [This is the MW of the unprocessed precursor]

CRC64: 48768B6EF204775A [This is a checksum on the sequence]

        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

P09582 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools