ID ESTA_CANLF Reviewed; 260 AA. AC P09582; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Arginine esterase; DE EC=3.4.21.35; DE Flags: Precursor; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Prostate; RX 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 of RT canine prostate."; RL FEBS Lett. 232:187-192(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1991049; DOI=10.1089/dna.1991.10.49; RA Chapdelaine P., Gauthier E., Ho-Kim M.-A., Bissonnette L., Tremblay R.R., RA Dube J.Y.; RT "Characterization and expression of the prostatic arginine esterase gene, a RT 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 PubMed=6566614; DOI=10.1016/0014-5793(84)80557-8; RA Lazure C., Leduc R., Seidah N.G., Chretien M., Dube J.Y., Chapdelaine P., RA 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 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: CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule CC substrates. Highly selective action to release kallidin (lysyl- CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|- CC Xaa.; EC=3.4.21.35; CC -!- INDUCTION: By androgens. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; NM_001003284.1. DR AlphaFoldDB; P09582; -. DR SMR; P09582; -. DR STRING; 9615.ENSCAFP00000065497; -. DR Allergome; 5762; Can f 5. DR Allergome; 5763; Can f 5.0101. DR MEROPS; S01.289; -. DR PaxDb; 9612-ENSCAFP00000004309; -. DR GeneID; 403967; -. DR KEGG; cfa:403967; -. DR CTD; 3817; -. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P09582; -. DR OrthoDB; 4629979at2759; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central. DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Reference proteome; Serine protease; Signal; Zymogen. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..24 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:6566614" FT /id="PRO_0000028019" FT CHAIN 25..260 FT /note="Arginine esterase" FT /id="PRO_0000028020" FT DOMAIN 25..257 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 65 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 119 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 212 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305" FT DISULFID 31..172 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 50..66 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 151..218 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 183..197 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 208..233 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CONFLICT 56 FT /note="N -> H (in Ref. 2; AAA30831)" FT /evidence="ECO:0000305" 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 //