ID   EST5A_HUMAN             Reviewed;         575 AA.
AC   Q6NT32; B7Z252; B7ZLB6; Q8NBC8; Q96DN9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 147.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Liu Q., Hamil K.G., French F.S., Hall S.H., Zhang Y.-L.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANT
RP   GLU-537.
RC   TISSUE=Amygdala, and Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6NT32-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NT32-2; Sequence=VSP_029006;
CC       Name=3;
CC         IsoId=Q6NT32-3; Sequence=VSP_029005;
CC       Name=4;
CC         IsoId=Q6NT32-4; Sequence=VSP_043296;
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was termed (Ref.1) CES5. {ECO:0000305}.
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DR   EMBL; AY907669; AAX86044.1; -; mRNA.
DR   EMBL; AK056109; BAB71094.1; -; mRNA.
DR   EMBL; AK090997; BAC03565.1; -; mRNA.
DR   EMBL; AK294334; BAH11738.1; -; mRNA.
DR   EMBL; AC007335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069501; AAH69501.1; -; mRNA.
DR   EMBL; BC069548; AAH69548.1; -; mRNA.
DR   EMBL; BC117126; AAI17127.1; -; mRNA.
DR   EMBL; BC143692; AAI43693.1; -; mRNA.
DR   CCDS; CCDS10755.1; -. [Q6NT32-2]
DR   CCDS; CCDS45490.1; -. [Q6NT32-1]
DR   CCDS; CCDS54012.1; -. [Q6NT32-4]
DR   RefSeq; NP_001137157.1; NM_001143685.1. [Q6NT32-1]
DR   RefSeq; NP_001177087.1; NM_001190158.1. [Q6NT32-4]
DR   RefSeq; NP_659461.1; NM_145024.2. [Q6NT32-2]
DR   AlphaFoldDB; Q6NT32; -.
DR   SMR; Q6NT32; -.
DR   STRING; 9606.ENSP00000428864; -.
DR   ESTHER; human-CES5A; Carb_B_Chordata.
DR   MEROPS; S09.960; -.
DR   GlyCosmos; Q6NT32; 4 sites, No reported glycans.
DR   GlyGen; Q6NT32; 4 sites.
DR   iPTMnet; Q6NT32; -.
DR   PhosphoSitePlus; Q6NT32; -.
DR   BioMuta; CES5A; -.
DR   DMDM; 74758113; -.
DR   MassIVE; Q6NT32; -.
DR   PaxDb; 9606-ENSP00000428864; -.
DR   PeptideAtlas; Q6NT32; -.
DR   ProteomicsDB; 66653; -. [Q6NT32-1]
DR   ProteomicsDB; 66654; -. [Q6NT32-2]
DR   ProteomicsDB; 66655; -. [Q6NT32-3]
DR   ProteomicsDB; 66656; -. [Q6NT32-4]
DR   Antibodypedia; 28532; 123 antibodies from 22 providers.
DR   DNASU; 221223; -.
DR   Ensembl; ENST00000290567.14; ENSP00000290567.9; ENSG00000159398.16. [Q6NT32-1]
DR   Ensembl; ENST00000319165.13; ENSP00000324271.9; ENSG00000159398.16. [Q6NT32-2]
DR   Ensembl; ENST00000518005.5; ENSP00000428571.1; ENSG00000159398.16. [Q6NT32-3]
DR   Ensembl; ENST00000521992.5; ENSP00000428864.1; ENSG00000159398.16. [Q6NT32-4]
DR   GeneID; 221223; -.
DR   KEGG; hsa:221223; -.
DR   MANE-Select; ENST00000290567.14; ENSP00000290567.9; NM_001143685.2; NP_001137157.1.
DR   UCSC; uc002eip.3; human. [Q6NT32-1]
DR   AGR; HGNC:26459; -.
DR   CTD; 221223; -.
DR   GeneCards; CES5A; -.
DR   HGNC; HGNC:26459; CES5A.
DR   HPA; ENSG00000159398; Tissue enriched (epididymis).
DR   MIM; 618678; gene.
DR   neXtProt; NX_Q6NT32; -.
DR   OpenTargets; ENSG00000159398; -.
DR   PharmGKB; PA142672130; -.
DR   VEuPathDB; HostDB:ENSG00000159398; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   GeneTree; ENSGT00940000161596; -.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; Q6NT32; -.
DR   OMA; HWIQQSP; -.
DR   OrthoDB; 4386at2759; -.
DR   PhylomeDB; Q6NT32; -.
DR   TreeFam; TF315470; -.
DR   PathwayCommons; Q6NT32; -.
DR   BioGRID-ORCS; 221223; 9 hits in 1142 CRISPR screens.
DR   ChiTaRS; CES5A; human.
DR   GenomeRNAi; 221223; -.
DR   Pharos; Q6NT32; Tbio.
DR   PRO; PR:Q6NT32; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q6NT32; Protein.
DR   Bgee; ENSG00000159398; Expressed in primordial germ cell in gonad and 43 other cell types or tissues.
DR   ExpressionAtlas; Q6NT32; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0106435; F:carboxylesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   PANTHER; PTHR11559; CARBOXYLESTERASE; 1.
DR   PANTHER; PTHR11559:SF43; CARBOXYLESTERASE 5A; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR   Genevisible; Q6NT32; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..575
FT                   /note="Carboxylesterase 5A"
FT                   /id="PRO_0000308591"
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        513
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   VAR_SEQ         1..106
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_029005"
FT   VAR_SEQ         1..24
FT                   /note="MSGNWVHPGQILIWAIWVLAAPTK -> MAVLVCPASCHGLKEFRIRRGMWR
FT                   LCLVYYFYPASSTLYVLRIDVLNYTSKDE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043296"
FT   VAR_SEQ         425..474
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029006"
FT   VARIANT         71
FT                   /note="R -> Q (in dbSNP:rs2397965)"
FT                   /id="VAR_036836"
FT   VARIANT         261
FT                   /note="E -> K (in dbSNP:rs11076126)"
FT                   /id="VAR_036837"
FT   VARIANT         344
FT                   /note="H -> Q (in dbSNP:rs11860946)"
FT                   /id="VAR_036838"
FT   VARIANT         499
FT                   /note="G -> R (in dbSNP:rs16955812)"
FT                   /id="VAR_036839"
FT   VARIANT         537
FT                   /note="D -> E (in dbSNP:rs11860456)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_036840"
FT   CONFLICT        343
FT                   /note="N -> S (in Ref. 2; BAC03565)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   575 AA;  63926 MW;  6F5B735BDEFC9C09 CRC64;
     MSGNWVHPGQ ILIWAIWVLA APTKGPSAEG PQRNTRLGWI QGKQVTVLGS PVPVNVFLGV
     PFAAPPLGSL RFTNPQPASP WDNLREATSY PNLCLQNSEW LLLDQHMLKV HYPKFGVSED
     CLYLNIYAPA HADTGSKLPV LVWFPGGAFK TGSASIFDGS ALAAYEDVLV VVVQYRLGIF
     GFFTTWDQHA PGNWAFKDQV AALSWVQKNI EFFGGDPSSV TIFGESAGAI SVSSLILSPM
     AKGLFHKAIM ESGVAIIPYL EAHDYEKSED LQVVAHFCGN NASDSEALLR CLRTKPSKEL
     LTLSQKTKSF TRVVDGAFFP NEPLDLLSQK AFKAIPSIIG VNNHECGFLL PMKEAPEILS
     GSNKSLALHL IQNILHIPPQ YLHLVANEYF HDKHSLTEIR DSLLDLLGDV FFVVPALITA
     RYHRDAGAPV YFYEFRHRPQ CFEDTKPAFV KADHADEVRF VFGGAFLKGD IVMFEGATEE
     EKLLSRKMMK YWATFARTGN PNGNDLSLWP AYNLTEQYLQ LDLNMSLGQR LKEPRVDFWT
     STIPLILSAS DMLHSPLSSL TFLSLLQPFF FFCAP
//