EST2C_MOUSE
ID EST2C_MOUSE Reviewed; 561 AA.
AC Q91WG0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Acylcarnitine hydrolase;
DE Short=ACH M1;
DE EC=3.1.1.28;
DE AltName: Full=Carboxylesterase 2;
DE Short=CES 2;
DE AltName: Full=Carboxylic ester hydrolase {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=Peroxisome proliferator-inducible acylcarnitine hydrolase;
DE Flags: Precursor;
GN Name=Ces2c {ECO:0000312|MGI:MGI:2385905}; Synonyms=Ces2;
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], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12859986; DOI=10.1016/s0003-9861(03)00286-8;
RA Furihata T., Hosokawa M., Nakata F., Satoh T., Chiba K.;
RT "Purification, molecular cloning, and functional expression of inducible
RT liver acylcarnitine hydrolase in C57BL/6 mouse, belonging to the
RT carboxylesterase multigene family.";
RL Arch. Biochem. Biophys. 416:101-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Kidney;
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=Kidney;
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: Hydrolase with high activity towards palmitoylcarnitine. Is
CC also active with p-nitrophenylacetate and alpha-naphthylacetate. May
CC also hydrolyze retinyl esters (By similarity).
CC {ECO:0000250|UniProtKB:O70631, ECO:0000269|PubMed:12859986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-acyl-(R)-carnitine = (R)-carnitine + a fatty acid +
CC H(+); Xref=Rhea:RHEA:17101, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:28868, ChEBI:CHEBI:75659; EC=3.1.1.28;
CC Evidence={ECO:0000269|PubMed:12859986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:O70631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:O70631};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=98.8 uM for palmitoyl-dl-carnitine;
CC KM=392 uM for p-nitrophenylacetate;
CC Vmax=1.67 umol/min/mg enzyme with palmitoyl-dl-carnitine;
CC Vmax=353 umol/min/mg enzyme with p-nitrophenylacetate;
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12859986}.
CC Endoplasmic reticulum {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:12859986}.
CC -!- INDUCTION: Up-regulated in liver by di-(2-ethylhexyl)phtalate (DEHP).
CC {ECO:0000269|PubMed:12859986}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AB110073; BAC76623.1; -; mRNA.
DR EMBL; AC156564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015290; AAH15290.1; -; mRNA.
DR EMBL; BC024552; AAH24552.1; -; mRNA.
DR EMBL; BC031170; AAH31170.1; -; mRNA.
DR EMBL; BC034178; AAH34178.1; -; mRNA.
DR EMBL; BC034180; AAH34180.1; -; mRNA.
DR EMBL; BC034191; AAH34191.1; -; mRNA.
DR CCDS; CCDS22587.1; -.
DR RefSeq; NP_663578.1; NM_145603.2.
DR AlphaFoldDB; Q91WG0; -.
DR SMR; Q91WG0; -.
DR STRING; 10090.ENSMUSP00000058567; -.
DR BindingDB; Q91WG0; -.
DR ChEMBL; CHEMBL2217; -.
DR ESTHER; mouse-Ces2c; Carb_B_Chordata.
DR MEROPS; S09.999; -.
DR iPTMnet; Q91WG0; -.
DR PhosphoSitePlus; Q91WG0; -.
DR jPOST; Q91WG0; -.
DR MaxQB; Q91WG0; -.
DR PaxDb; Q91WG0; -.
DR PeptideAtlas; Q91WG0; -.
DR PRIDE; Q91WG0; -.
DR ProteomicsDB; 275649; -.
DR DNASU; 234671; -.
DR Ensembl; ENSMUST00000055052; ENSMUSP00000058567; ENSMUSG00000061825.
DR GeneID; 234671; -.
DR KEGG; mmu:234671; -.
DR UCSC; uc009nbe.2; mouse.
DR CTD; 234671; -.
DR MGI; MGI:2385905; Ces2c.
DR VEuPathDB; HostDB:ENSMUSG00000061825; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000153793; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q91WG0; -.
DR OMA; SHPNDLF; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q91WG0; -.
DR TreeFam; TF315470; -.
DR BioGRID-ORCS; 234671; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ces2c; mouse.
DR PRO; PR:Q91WG0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WG0; protein.
DR Bgee; ENSMUSG00000061825; Expressed in proximal tubule and 26 other tissues.
DR Genevisible; Q91WG0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0047619; F:acylcarnitine hydrolase activity; IDA:UniProtKB.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISO:MGI.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISO:MGI.
DR GO; GO:1903412; P:response to bile acid; IDA:MGI.
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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Hydrolase; Lipid metabolism; Microsome; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..561
FT /note="Acylcarnitine hydrolase"
FT /id="PRO_5000396880"
FT MOTIF 558..561
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 230
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|UniProtKB:P23141"
FT ACT_SITE 459
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 97..125
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 282..293
FT /evidence="ECO:0000250|UniProtKB:P23141"
SQ SEQUENCE 561 AA; 62470 MW; F793967A646EB728 CRC64;
MTRNQLHNWL NAGFFGLLLL LIHVQGQDSP EANPIRNTHT GQIQGSLIHV KDTKAGVHTF
LGIPFAKPPV GPLRFAPPEA PEPWSGVRDG TAHPAMCLQN LDMLNEAGLP DMKMMLSSFP
MSEDCLYLNI YTPAHAHEGS NLPVMVWIHG GALVIGMASM FDGSLLTVNE DLVVVTIQYR
LGVLGFFSTG DQHARGNWGY LDQAAALRWV QQNIAHFGGN PDRVTIFGES AGGTSVSSHV
VSPMSQGLFH GAIMESGVAL LPDLISETSE MVSTTVAKLS GCEAMDSQAL VRCLRGKSEA
EILAINKVFK MIPAVVDGEF FPRHPKELLA SEDFHPVPSI IGVNNDEFGW SIPVVMGSAQ
MIKGITRENL QAVLKDTAVQ MMLPPECSDL LMEEYMGDTE DAQTLQIQFT EMMGDFMFVI
PALQVAHFQR SHAPVYFYEF QHPPSYFKDV RPPHVKADHA DEIPFVFASF FWGMKLDFTE
EEELLSRRMM KYWANFARHG NPNSEGLPYW PVMDHDEQYL QLDIQPAVGR ALKAGRLQFW
TKTLPQKIQE LKASQDKHRE L
