ID   EST5A_MOUSE             Reviewed;         575 AA.
AC   Q6AW46;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
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; AB186393; BAD35016.1; -; mRNA.
DR   CCDS; CCDS85584.1; -.
DR   RefSeq; NP_001003951.1; NM_001003951.2.
DR   AlphaFoldDB; Q6AW46; -.
DR   SMR; Q6AW46; -.
DR   STRING; 10090.ENSMUSP00000076988; -.
DR   ESTHER; mouse-cauxin; Carb_B_Chordata.
DR   GlyGen; Q6AW46; 4 sites.
DR   PhosphoSitePlus; Q6AW46; -.
DR   jPOST; Q6AW46; -.
DR   MaxQB; Q6AW46; -.
DR   PaxDb; Q6AW46; -.
DR   PeptideAtlas; Q6AW46; -.
DR   PRIDE; Q6AW46; -.
DR   ProteomicsDB; 275691; -.
DR   Antibodypedia; 28532; 116 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000077816; ENSMUSP00000076988; ENSMUSG00000058019.
DR   Ensembl; ENSMUST00000212009; ENSMUSP00000148481; ENSMUSG00000058019.
DR   GeneID; 67935; -.
DR   KEGG; mmu:67935; -.
DR   UCSC; uc033jgu.1; mouse.
DR   CTD; 221223; -.
DR   MGI; MGI:1915185; Ces5a.
DR   VEuPathDB; HostDB:ENSMUSG00000058019; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   GeneTree; ENSGT00940000161596; -.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; Q6AW46; -.
DR   OMA; KWFDLHR; -.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; Q6AW46; -.
DR   TreeFam; TF315470; -.
DR   BioGRID-ORCS; 67935; 3 hits in 66 CRISPR screens.
DR   PRO; PR:Q6AW46; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q6AW46; protein.
DR   Bgee; ENSMUSG00000058019; Expressed in lumbar dorsal root ganglion and 30 other tissues.
DR   ExpressionAtlas; Q6AW46; baseline and differential.
DR   Genevisible; Q6AW46; MM.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..575
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308592"
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        134
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;  64167 MW;  3EB9D85981D9DE0A CRC64;
     MSGDWVRPGQ ALIWVIWIFG AIIEGSVTEE PHRYTKLGWV QGKQATVLGR LEPVNVFLGI
     PFAAPPLGPL RFSKPQPPIP WDNLREATAY PNLCFQNLEW LFIYQNLLKV SYPILGMSED
     CLYLNIYAPC HANNGSSLPV MVWIPGGGFE TGSASIFDGS ALAVYEDVLV VTIQYRLGIF
     GFFTTQNQHA PGNWAFWDQL AALLWVRENI KYFGGNPDSV TIFGNSAGAI SISSLILSPL
     SADLFHRAIM QSGVAIIPSL KSSDNDLKHD LQVVANVCDC NVSDSKALLK CLREKSSLEL
     MSLSQKAKSF TRVVDGSFFS EEPLELLSQK TLKIVPSIIG VNNQECGYIL PVRDTPEILL
     GSNESTALTL IHTLLHIPTQ HLYIVTKEYF HGKHSPTDIR DTLLDLFGDV FFVVPGLVTA
     RYHRDSGGPV YFYEFQHRPH CFQNSRPAFV KADHTDEIRF VFGGPFLKGD VVMFEEATEE
     EKLLSRKMMK YWANFARSGD PNGADLPPWP VYDENEQYLE LDVNISTGRR LKDQRVEFWT
     DTLPLILSAS KALLSPTFSL ILLSLLSPVL LSAAS