EST3A_MOUSE
ID EST3A_MOUSE Reviewed; 571 AA.
AC Q63880; Q3UEJ0; Q3UU08; Q6P8Z0; Q6PG74; Q810S9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Carboxylesterase 3A;
DE EC=3.1.1.1;
DE AltName: Full=ES-male;
DE AltName: Full=Liver carboxylesterase 31;
DE Short=Esterase-31;
DE Flags: Precursor;
GN Name=Ces3a; Synonyms=Es31;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=BALB/CJ X DBA/2J; TISSUE=Liver;
RX PubMed=7916639; DOI=10.1016/0167-4781(93)90093-s;
RA Aida K., Moore R., Negishi M.;
RT "Cloning and nucleotide sequence of a novel, male-predominant
RT carboxylesterase in mouse liver.";
RL Biochim. Biophys. Acta 1174:72-74(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs.
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: Endoplasmic reticulum lumen. Note=Microsomal
CC membrane, lumen of endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63880-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63880-2; Sequence=VSP_028268;
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB27606.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH57187.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH57188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S64130; AAB27606.1; ALT_FRAME; mRNA.
DR EMBL; AK138932; BAE23821.1; -; mRNA.
DR EMBL; AK149499; BAE28921.1; -; mRNA.
DR EMBL; BC048380; AAH48380.1; -; mRNA.
DR EMBL; BC057187; AAH57187.1; ALT_INIT; mRNA.
DR EMBL; BC057188; AAH57188.1; ALT_INIT; mRNA.
DR EMBL; BC061004; AAH61004.2; -; mRNA.
DR CCDS; CCDS52651.1; -. [Q63880-1]
DR CCDS; CCDS52652.1; -. [Q63880-2]
DR PIR; S34607; S34607.
DR RefSeq; NP_001158153.1; NM_001164681.1. [Q63880-2]
DR RefSeq; NP_941074.1; NM_198672.1. [Q63880-1]
DR AlphaFoldDB; Q63880; -.
DR SMR; Q63880; -.
DR BioGRID; 238210; 1.
DR IntAct; Q63880; 1.
DR STRING; 10090.ENSMUSP00000090910; -.
DR ESTHER; mouse-Ces3a; Carb_B_Chordata.
DR MEROPS; S09.964; -.
DR GlyGen; Q63880; 3 sites.
DR iPTMnet; Q63880; -.
DR PhosphoSitePlus; Q63880; -.
DR SwissPalm; Q63880; -.
DR CPTAC; non-CPTAC-3802; -.
DR jPOST; Q63880; -.
DR MaxQB; Q63880; -.
DR PaxDb; Q63880; -.
DR PeptideAtlas; Q63880; -.
DR PRIDE; Q63880; -.
DR ProteomicsDB; 275650; -. [Q63880-1]
DR ProteomicsDB; 275651; -. [Q63880-2]
DR DNASU; 382053; -.
DR Ensembl; ENSMUST00000093222; ENSMUSP00000090910; ENSMUSG00000069922. [Q63880-1]
DR Ensembl; ENSMUST00000093223; ENSMUSP00000090911; ENSMUSG00000069922. [Q63880-2]
DR GeneID; 382053; -.
DR KEGG; mmu:382053; -.
DR UCSC; uc009nbl.2; mouse. [Q63880-1]
DR UCSC; uc009nbm.2; mouse. [Q63880-2]
DR CTD; 382053; -.
DR MGI; MGI:102773; Ces3a.
DR VEuPathDB; HostDB:ENSMUSG00000069922; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000155200; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q63880; -.
DR OMA; IFFYEFQ; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q63880; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 3474.
DR BioGRID-ORCS; 382053; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ces3a; mouse.
DR PRO; PR:Q63880; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q63880; protein.
DR Bgee; ENSMUSG00000069922; Expressed in hepatobiliary system and 31 other tissues.
DR Genevisible; Q63880; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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 Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..571
FT /note="Carboxylesterase 3A"
FT /id="PRO_0000008575"
FT MOTIF 568..571
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 460
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..127
FT /evidence="ECO:0000250"
FT DISULFID 284..295
FT /evidence="ECO:0000250"
FT VAR_SEQ 307..353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028268"
FT CONFLICT 156
FT /note="L -> R (in Ref. 1; AAB27606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63318 MW; 9036F8946BEA85CE CRC64;
MTNMETTAQA GSSVRVWMAC LLLIFPTTVI GPKVTQPEVD TPLGRVRGRQ VGVKDTDRMV
NVFLGIPFAQ APLGPLRFSA PLPPQPWEGV RDASINPPMC LQDVERMSNS RFTLNEKMKI
FPISEDCLTL NIYSPTEITA GDKRPVMVWI HGGSLLVGSS TSHDGSALAA YGDVVVVTVQ
YRLGIFGFLS TGDKHMPGNR GFLDVVAALR WVQGNIAPFG GDPNCVTIFG NSAGGIIVSS
LLLSPMSAGL FHRAISQSGV VISKILEDLN AWSEAQNFAN SVACGSASPA ELVQCLLQKE
GKDLITKKNV NISYTVNDSF FPQRPQKLLA NKQFPTVPYL LGVTNHEFGW LLLKFWNILD
KMEHLSQEDL LENSRPLLAH MQLPPEIMPT VIDEYLDNGS DESATRYALQ ELLGDITLVI
PTLIFSKYLQ DAGCPVFLYE FQHTPSSFAK FKPAWVKADH SSENAFVFGG PFLTDESSLL
AFPEATEEEK QLSLTMMAQW SQFARTGNPN GKGLPPWPQL NQLEQYLEIG LEPRTGVKLK
KGRLQFWTET LPRKIQEWHR EQRSRKVPEE L
