ID   EST5A_CANLF             Reviewed;         575 AA.
AC   Q6AW47;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Carboxylesterase 5A;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylesterase-like urinary excreted protein homolog;
DE            Short=Cauxin;
DE   Flags: Precursor;
GN   Name=CES5A; Synonyms=CES7;
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].
RX   PubMed=17045831; DOI=10.1016/j.cbpb.2006.05.015;
RA   Miyazaki M., Yamashita T., Hosokawa M., Taira H., Suzuki A.;
RT   "Species-, sex-, and age-dependent urinary excretion of cauxin, a mammalian
RT   carboxylesterase.";
RL   Comp. Biochem. Physiol. 145B:270-277(2006).
CC   -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC       activation of ester and amide prodrugs. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AB186392; BAD35015.1; -; mRNA.
DR   RefSeq; NP_001003969.1; NM_001003969.1.
DR   AlphaFoldDB; Q6AW47; -.
DR   SMR; Q6AW47; -.
DR   STRING; 9615.ENSCAFP00000056757; -.
DR   ESTHER; canfa-cauxin; Carb_B_Chordata.
DR   PaxDb; Q6AW47; -.
DR   GeneID; 445456; -.
DR   KEGG; cfa:445456; -.
DR   CTD; 221223; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   InParanoid; Q6AW47; -.
DR   OrthoDB; 754103at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW   Serine esterase; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..575
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308589"
FT   ACT_SITE        226
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        454
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..291
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   575 AA;  63621 MW;  1005C35E82E1183D CRC64;
     MSGEWGHLGQ TLIWAVWVLA AATEGPAADA PVRSTRLGWV RGKQATVLGS TMPVNVFLGI
     PFAAPPLGPL RFKRPKPALL WNDSRDATSY PKLCLQNSVW LLSDQHFLKV HYPNLEVSED
     CLYLNIYAPA HANTGSKLPV MVWFPGGAFE TGSASIFDGS ALAAYEDVLI VTTQYRLGIF
     GFFKTGDQHA PGNWAFLDQL AALTWVQENI EFFGGDPHSV TIFGESAGAI SVSGLVLSPM
     ASGLFHKAIM ESGVAIIPFL RAPDDERNED LQVIARICGC NVSDSVALLQ CLRAKSSEEL
     LDINKKTKSF TRVVDGFFFP DEPLDLLTEK TFNSIPSVIG VNNHECGFLL PMKEFPEILG
     GSNKSLALHL IHRVLHIPNQ YLYLVADQYF YNKHSPVEIR DSFLDLLGDV FFVVPGVVTA
     RYHRDAGAPV YFYEFQHPPE CLKDTRPAFV KADHSDEIRF VFGGAFLKGN IVMFEGATEE
     EKLLSRKMMR YWANFARTGD PNGEGLPLWP AYSQSEQYLK LDLNISVGQK LKEQEVEFWS
     DTLPLIMSMS TAPPGPPVPL LSLSVLLPFL FSSAP