MBLC2_MOUSE
ID MBLC2_MOUSE Reviewed; 279 AA.
AC Q8BL86; G3X997;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acyl-coenzyme A thioesterase MBLAC2;
DE Short=Acyl-CoA thioesterase MBLAC2;
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q68D91};
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q68D91};
DE AltName: Full=Metallo-beta-lactamase domain-containing protein 2;
DE AltName: Full=Palmitoyl-coenzyme A thioesterase MBLAC2;
GN Name=Mblac2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 [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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Heart;
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: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC (CoASH), providing the potential to regulate intracellular levels of
CC acyl-CoAs, free fatty acids and CoASH. Has an acyl-CoA thioesterase
CC activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA
CC (hexadecanoyl-CoA; C16:0-CoA). Displays a substrate preference for
CC fatty acyl-CoAs with chain-lengths C12-C18.
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q68D91};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q68D91}. Cell membrane
CC {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- PTM: Palmitoylated on Cys-254 by ZDHHC20.
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AK046032; BAC32577.1; -; mRNA.
DR EMBL; AC154771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466563; EDL37142.1; -; Genomic_DNA.
DR CCDS; CCDS26662.1; -.
DR RefSeq; NP_082648.1; NM_028372.1.
DR AlphaFoldDB; Q8BL86; -.
DR SMR; Q8BL86; -.
DR STRING; 10090.ENSMUSP00000051644; -.
DR iPTMnet; Q8BL86; -.
DR PhosphoSitePlus; Q8BL86; -.
DR SwissPalm; Q8BL86; -.
DR EPD; Q8BL86; -.
DR MaxQB; Q8BL86; -.
DR PaxDb; Q8BL86; -.
DR PeptideAtlas; Q8BL86; -.
DR PRIDE; Q8BL86; -.
DR ProteomicsDB; 295970; -.
DR Antibodypedia; 50739; 18 antibodies from 8 providers.
DR DNASU; 72852; -.
DR Ensembl; ENSMUST00000057598; ENSMUSP00000051644; ENSMUSG00000051098.
DR GeneID; 72852; -.
DR KEGG; mmu:72852; -.
DR UCSC; uc007ria.1; mouse.
DR CTD; 153364; -.
DR MGI; MGI:1920102; Mblac2.
DR VEuPathDB; HostDB:ENSMUSG00000051098; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00390000017819; -.
DR HOGENOM; CLU_030571_0_2_1; -.
DR InParanoid; Q8BL86; -.
DR OMA; VASHTHF; -.
DR OrthoDB; 1203911at2759; -.
DR PhylomeDB; Q8BL86; -.
DR TreeFam; TF319889; -.
DR BioGRID-ORCS; 72852; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8BL86; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BL86; protein.
DR Bgee; ENSMUSG00000051098; Expressed in ventromedial nucleus of hypothalamus and 219 other tissues.
DR ExpressionAtlas; Q8BL86; baseline and differential.
DR Genevisible; Q8BL86; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Endoplasmic reticulum; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT CHAIN 2..279
FT /note="Acyl-coenzyme A thioesterase MBLAC2"
FT /id="PRO_0000325936"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT LIPID 254
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT CONFLICT 140
FT /note="V -> M (in Ref. 1; BAC32577)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Q -> P (in Ref. 1; BAC32577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 31205 MW; 76E976E24255BAF0 CRC64;
MSALEWYAHK SLGDGIFWIQ ERFYESGNRA NIWLVRGSEQ DVVIDTGLGL RSLPEYLYSS
GLLQDCGSKE DAGRRPLLAV ATHVHFDHSG GLYQFDQVAV HRAEAEALAR GDNFETVTWL
SDSEVVRAPS PGWRARQFRV QAVQPTLILQ DGDVINLGDR QLTVMHMPGH SRGSICLHDK
DRKVLFSGDV VYDGSLIDWL PYSRISDYVG TCERLIELVD RGLVEKVLPG HFNTFGAERL
FRLASNYISK AGICHKVSTF AMRSLASLAL RVTNPRTSP
