ID ESTA_CANFA Reviewed; 260 AA. AC P09582; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 26-MAY-2009, entry version 77. DE RecName: Full=Arginine esterase; DE EC=3.4.21.35; DE Flags: Precursor; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Prostate; RX MEDLINE=88211858; PubMed=2835268; DOI=10.1016/0014-5793(88)80414-9; RA Chapdelaine P., Ho-Kim M.-A., Tremblay R.R., Dube J.Y.; RT "Nucleotide sequence of the androgen-dependent arginine esterase mRNA RT of canine prostate."; RL FEBS Lett. 232:187-192(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91119675; PubMed=1991049; DOI=10.1089/dna.1991.10.49; RA Chapdelaine P., Gauthier E., Ho-Kim M.-A., Bissonnette L., RA Tremblay R.R., Dube J.Y.; RT "Characterization and expression of the prostatic arginine esterase RT gene, a canine glandular kallikrein."; RL DNA Cell Biol. 10:49-59(1991). RN [3] RP PROTEIN SEQUENCE OF 25-50 AND 108-145. RC TISSUE=Prostate; RX MEDLINE=85004070; PubMed=6566614; DOI=10.1016/0014-5793(84)80557-8; RA Lazure C., Leduc R., Seidah N.G., Chretien M., Dube J.Y., RA Chapdelaine P., Frenette G., Paquin R., Tremblay R.R.; RT "The major androgen-dependent protease in dog prostate belongs to the RT kallikrein family: confirmation by partial amino acid sequencing."; RL FEBS Lett. 175:1-7(1984). RN [4] RP NUCLEOTIDE SEQUENCE OF 105-260. RX MEDLINE=88225749; PubMed=3371547; DOI=10.1016/0303-7207(88)90009-3; RA Chapdelaine P., Potvin C., Ho-Kim M.A., Larouche L., Bellemare G., RA Tremblay R.T., Dube J.Y.; RT "Androgen regulation of canine prostatic arginine esterase mRNA using RT cloned cDNA."; RL Mol. Cell. Endocrinol. 56:63-70(1988). CC -!- FUNCTION: This serine protease is found in dog seminal plasma, its CC exact physiological function is not known. CC -!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in CC small molecule substrates. Highly selective action to release CC kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of CC Met-|-Xaa or Leu-|-Xaa. CC -!- INDUCTION: By androgens. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein CC subfamily. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00751; CAA68720.1; -; mRNA. DR EMBL; M63669; AAA30831.1; -; Genomic_DNA. DR PIR; A30981; A30981. DR PIR; A37938; A37938. DR RefSeq; NP_001003284.1; -. DR UniGene; Cfa.3836; -. DR HSSP; P00752; 2PKA. DR MEROPS; S01.289; -. DR GeneID; 403967; -. DR KEGG; cfa:403967; -. DR HOVERGEN; P09582; -. DR BRENDA; 3.4.21.35; 463. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; KW Protease; Serine protease; Signal; Zymogen. FT SIGNAL 1 17 Potential. FT PROPEP 18 24 Activation peptide. FT /FTId=PRO_0000028019. FT CHAIN 25 260 Arginine esterase. FT /FTId=PRO_0000028020. FT DOMAIN 25 257 Peptidase S1. FT ACT_SITE 65 65 Charge relay system (By similarity). FT ACT_SITE 119 119 Charge relay system (By similarity). FT ACT_SITE 212 212 Charge relay system (By similarity). FT CARBOHYD 79 79 N-linked (GlcNAc...) (Probable). FT DISULFID 31 172 By similarity. FT DISULFID 50 66 By similarity. FT DISULFID 151 218 By similarity. FT DISULFID 183 197 By similarity. FT DISULFID 208 233 By similarity. FT CONFLICT 56 56 N -> H (in Ref. 2; AAA30831). SQ SEQUENCE 260 AA; 28746 MW; 48768B6EF204775A CRC64; MWFLALCLAM SLGWTGAEPH FQPRIIGGRE CLKNSQPWQV AVYHNGEFAC GGVLVNPEWV LTAAHCANSN CEVWLGRHNL SESEDEGQLV QVRKSFIHPL YKTKVPRAVI RPGEDRSHDL MLLHLEEPAK ITKAVRVMDL PKKEPPLGST CYVSGWGSTD PETIFHPGSL QCVDLKLLSN NQCAKVYTQK VTKFMLCAGV LEGKKDTCKG DSGGPLICDG ELVGITSWGA TPCGKPQMPS LYTRVMPHLM WIKDTMKANT //