EST5A_HUMAN
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 03-AUG-2022, entry version 140.
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 GlyGen; Q6NT32; 4 sites.
DR iPTMnet; Q6NT32; -.
DR PhosphoSitePlus; Q6NT32; -.
DR BioMuta; CES5A; -.
DR DMDM; 74758113; -.
DR MassIVE; Q6NT32; -.
DR PaxDb; Q6NT32; -.
DR PeptideAtlas; Q6NT32; -.
DR PRIDE; Q6NT32; -.
DR ProteomicsDB; 66653; -. [Q6NT32-1]
DR ProteomicsDB; 66654; -. [Q6NT32-2]
DR ProteomicsDB; 66655; -. [Q6NT32-3]
DR ProteomicsDB; 66656; -. [Q6NT32-4]
DR Antibodypedia; 28532; 116 antibodies from 21 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 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; KWFDLHR; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q6NT32; -.
DR TreeFam; TF315470; -.
DR PathwayCommons; Q6NT32; -.
DR BioGRID-ORCS; 221223; 7 hits in 1064 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 right lobe of liver and 41 other tissues.
DR ExpressionAtlas; Q6NT32; baseline and differential.
DR Genevisible; Q6NT32; HS.
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 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
