ID   EST5A_RAT               Reviewed;         575 AA.
AC   Q5GRG2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Carboxylesterase 5A;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylesterase-like urinary excreted protein homolog;
DE            Short=Cauxin;
DE   AltName: Full=Epididymis-specific gene 615 protein;
DE   Flags: Precursor;
GN   Name=Ces5a; Synonyms=Ces7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epididymis;
RA   Hu Z.-H., Zhang Y.-L.;
RT   "Identification of rat epididymis-specific gene 615.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19727521; DOI=10.1093/abbs/gmp061;
RA   Zhang L., Liu Q., Zhou Y., Zhang Y.;
RT   "Baculo-expression and enzymatic characterization of CES7 esterase.";
RL   Acta Biochim. Biophys. Sin. 41:731-736(2009).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=670 uM for p-NPA {ECO:0000269|PubMed:19727521};
CC         Vmax=200 umol/min/mg enzyme with p-NPA as substrate
CC         {ECO:0000269|PubMed:19727521};
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:19727521};
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}.
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; AF479659; AAQ05814.1; -; mRNA.
DR   RefSeq; NP_001012056.1; NM_001012056.1.
DR   AlphaFoldDB; Q5GRG2; -.
DR   SMR; Q5GRG2; -.
DR   STRING; 10116.ENSRNOP00000045129; -.
DR   ESTHER; ratno-cauxin; Carb_B_Chordata.
DR   GlyGen; Q5GRG2; 4 sites.
DR   PaxDb; Q5GRG2; -.
DR   PRIDE; Q5GRG2; -.
DR   GeneID; 307660; -.
DR   KEGG; rno:307660; -.
DR   UCSC; RGD:1549717; rat.
DR   CTD; 221223; -.
DR   RGD; 1549717; Ces5a.
DR   eggNOG; KOG1516; Eukaryota.
DR   InParanoid; Q5GRG2; -.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; Q5GRG2; -.
DR   PRO; PR:Q5GRG2; -.
DR   Proteomes; UP000002494; 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; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..575
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308593"
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        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        515
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;  64417 MW;  61E4404845225D47 CRC64;
     MSGDWVHTGQ ALIWVLWIFA AIIRGSVTEE PHRYTRLGWV QGKQATVLGR LEPVNVFLGI
     PFAAPPLGPL RFSNPQPPIP WHDLREATTY PNVCFQNLEW LFIYQNLLKV HYPKLGVSED
     CLYLNIYAPA YANDGSRLPV MMWIPGGGFE TGSASIFDGS ALAAYEDVLI VTIQYRLGIF
     GFFNTQNQHA PGNWAFQDQL AALQWVRENI NYFGGNPDSV TIFGGSAGAI SISSLILSPL
     SAGLFHRAIM QSGVAIIPSL KNFDDELKHG LQVVADVCKC NVSDSKVLLK CLREKSSLEL
     LSLGQKTKAF TRVVDGSFFP EEPMELLSQK TFKTVPSIIG VNNQECGYIL PMREAPEILF
     GSNESTALTL IHVLLHIPPQ YMHIVAKDYF HGKHSLTDIR DTLLDLFGDV FFVVPGLVTA
     RNHRDADGPV YFYEFQHRPN CFQNTRPAFV KADHTDEIRF VFGGPFLEGD VVMFEEATED
     EKLLSRKMMS YWANFARSGD PNGDDLPLWP AYDQNESYLK LDVNISTGWR LKDRRVEFWT
     DTLPLIMSAS KALLSPTFPL ILFSLLPPSL LSIAS