ABHEB_MOUSE
ID ABHEB_MOUSE Reviewed; 210 AA.
AC Q8VCR7;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Putative protein-lysine deacylase ABHD14B {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q96IU4};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 14B {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 14B {ECO:0000250|UniProtKB:Q96IU4};
GN Name=Abhd14b {ECO:0000312|MGI:MGI:1923741};
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 TISSUE=Salivary gland;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Acts as an atypical protein-lysine deacetylase in vitro.
CC Catalyzes the deacetylation of lysine residues using CoA as substrate,
CC generating acetyl-CoA and the free amine of protein-lysine residues.
CC Additional experiments are however required to confirm the protein-
CC lysine deacetylase activity in vivo. Has hydrolase activity towards
CC various surrogate p-nitrophenyl (pNp) substrates, such as pNp-butyrate,
CC pNp-acetate and pNp-octanoate in vitro, with a strong preference for
CC pNp-acetate. May activate transcription.
CC {ECO:0000250|UniProtKB:Q96IU4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000250|UniProtKB:Q96IU4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45950;
CC Evidence={ECO:0000250|UniProtKB:Q96IU4};
CC -!- SUBUNIT: May interact with TAF1. {ECO:0000250|UniProtKB:Q96IU4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96IU4}. Nucleus
CC {ECO:0000250|UniProtKB:Q96IU4}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q96IU4}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD14 family.
CC {ECO:0000305}.
CC -!- CAUTION: The protein-lysine deacetylase activity using CoA as substrate
CC is unclear as this protein belongs to a family of serine hydrolases,
CC and that the reaction shown in the publication is not hydrolyzing H(2)O
CC (By similarity). Additional experiments are therefore required to
CC confirm this activity in vivo (By similarity).
CC {ECO:0000250|UniProtKB:Q96IU4}.
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DR EMBL; BC019410; AAH19410.1; -; mRNA.
DR CCDS; CCDS23478.1; -.
DR AlphaFoldDB; Q8VCR7; -.
DR SMR; Q8VCR7; -.
DR STRING; 10090.ENSMUSP00000038755; -.
DR ESTHER; mouse-c1ib; CIB-CCG1-interacting-factor-B.
DR MEROPS; S33.983; -.
DR iPTMnet; Q8VCR7; -.
DR PhosphoSitePlus; Q8VCR7; -.
DR SwissPalm; Q8VCR7; -.
DR EPD; Q8VCR7; -.
DR jPOST; Q8VCR7; -.
DR MaxQB; Q8VCR7; -.
DR PaxDb; Q8VCR7; -.
DR PeptideAtlas; Q8VCR7; -.
DR PRIDE; Q8VCR7; -.
DR ProteomicsDB; 285908; -.
DR MGI; MGI:1923741; Abhd14b.
DR eggNOG; ENOG502QR0B; Eukaryota.
DR InParanoid; Q8VCR7; -.
DR PhylomeDB; Q8VCR7; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR ChiTaRS; Abhd14b; mouse.
DR PRO; PR:Q8VCR7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VCR7; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..210
FT /note="Putative protein-lysine deacylase ABHD14B"
FT /id="PRO_0000065039"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96IU4"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96IU4"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96IU4"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96IU4"
SQ SEQUENCE 210 AA; 22451 MW; EA3A15AF01288120 CRC64;
MAGVDQHEGT IQVQGQNLFF RETRPGSGQP VRFSVLLLHG IRFSSETWQN LGTLQRLAEA
GYRAVAIDLP GLGRSKEAAA PAPIGEPAPG SFLAAVVDTL ELGPPVVISP SLSGMYSLPF
LVAPGSQLRG FVPVAPICTD KINAVDYASV KTPALIVYGD QDPMGSSSFQ HLKQLPNHRV
LVMEGAGHPC YLDKPDEWHK GLLDFLQGLA
