ID   EST5A_SHEEP             Reviewed;         381 AA.
AC   Q3T930;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
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: Fragment;
GN   Name=CES5A; Synonyms=CES7;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   IDENTIFICATION IN COMPLEX WITH PRNP; CLU; BPI; MANBA AND GLB1.
RC   TISSUE=Epididymis;
RX   PubMed=16029166; DOI=10.1042/bj20050459;
RA   Ecroyd H., Belghazi M., Dacheux J.-L., Gatti J.-L.;
RT   "The epididymal soluble prion protein forms a high-molecular-mass complex
RT   in association with hydrophobic proteins.";
RL   Biochem. J. 392:211-219(2005).
RN   [2]
RP   ENZYME ACTIVITY, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=16251497; DOI=10.1095/biolreprod.105.046847;
RA   Ecroyd H., Belghazi M., Dacheux J.-L., Miyazaki M., Yamashita T.,
RA   Gatti J.-L.;
RT   "An epididymal form of cauxin, a carboxylesterase-like enzyme, is present
RT   and active in mammalian male reproductive fluids.";
RL   Biol. Reprod. 74:439-447(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         ECO:0000269|PubMed:16251497};
CC   -!- SUBUNIT: Component of a epididymal complex at least composed of soluble
CC       form of prion protein PRNP, CLU, BPI, CES5A, MANBA and GLB1.
CC       {ECO:0000269|PubMed:16029166}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in corpus and cauda epididymal fluid.
CC       Present in seminal fluid but not found to be associated with sperm (at
CC       protein level). Not expressed in other tissues.
CC       {ECO:0000269|PubMed:16251497}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16251497}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AM075621; CAJ27151.1; -; mRNA.
DR   AlphaFoldDB; Q3T930; -.
DR   SMR; Q3T930; -.
DR   STRING; 9940.ENSOARP00000019937; -.
DR   ESTHER; sheep-cauxin; Carb_B_Chordata.
DR   eggNOG; KOG1516; Eukaryota.
DR   Proteomes; UP000002356; 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   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW   Serine esterase.
FT   CHAIN           <1..>381
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308594"
FT   ACT_SITE        108
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        336
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        162..173
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         381
SQ   SEQUENCE   381 AA;  42468 MW;  38F19BDADD346EA4 CRC64;
     EDCLYLNIYA PAHAETGSKL PVMVWFPGGA FETGSASIFD GSALASYENV LVVTIQYRLG
     IFGFFNTGDE HARGNWAFMD QVAALVWVQE NIEFFGGDPR CVTIFGESAG AISVSSLILS
     PMTKGLFHKA IMASGVAIIP YLKASDYERN DDLQTIASIC DCNASDSVAL LQCLRAKSSE
     ELLSISQKTK SFTRVVDGLF FPNELLDLLA QKLFHLVPSI IGVNNHECGF LLPMKEFPEI
     LGGSNKSLAL QLIHSVLHIP VQYSYLVADE YFHNKHSLLD IRNRFLDLLG DVFFVVPGLV
     TAQYHTDAGA PVYFYEFQHR PQCLKDRKPP FVKADHTDEI RFVFGGAFLK GNIVMFEEAT
     EEEKALSRKM MRYWANFART G