ESTA_CANLF
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 25-MAY-2022, entry version 119.
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}.
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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; 9612.ENSCAFP00000004309; -.
DR Allergome; 5762; Can f 5.
DR Allergome; 5763; Can f 5.0101.
DR MEROPS; S01.289; -.
DR PaxDb; P09582; -.
DR GeneID; 403967; -.
DR KEGG; cfa:403967; -.
DR CTD; 3817; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000002254; 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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 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
