ABHEB_BOVIN
ID ABHEB_BOVIN Reviewed; 210 AA.
AC A7YY28;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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:0000250|UniProtKB:Q96IU4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BC149237; AAI49238.1; -; mRNA.
DR RefSeq; NP_001098911.1; NM_001105441.1.
DR RefSeq; XP_005222981.1; XM_005222924.3.
DR AlphaFoldDB; A7YY28; -.
DR SMR; A7YY28; -.
DR STRING; 9913.ENSBTAP00000024782; -.
DR ESTHER; bovin-abheb; CIB-CCG1-interacting-factor-B.
DR MEROPS; S33.983; -.
DR PaxDb; A7YY28; -.
DR PeptideAtlas; A7YY28; -.
DR PRIDE; A7YY28; -.
DR Ensembl; ENSBTAT00000024782; ENSBTAP00000024782; ENSBTAG00000037377.
DR GeneID; 615289; -.
DR KEGG; bta:615289; -.
DR CTD; 84836; -.
DR VEuPathDB; HostDB:ENSBTAG00000037377; -.
DR VGNC; VGNC:25493; ABHD14B.
DR eggNOG; ENOG502QR0B; Eukaryota.
DR GeneTree; ENSGT00940000159388; -.
DR HOGENOM; CLU_020336_28_0_1; -.
DR InParanoid; A7YY28; -.
DR OMA; VQVESCN; -.
DR OrthoDB; 616687at2759; -.
DR TreeFam; TF314465; -.
DR Reactome; R-BTA-156584; Cytosolic sulfonation of small molecules.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000037377; Expressed in thyroid gland and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..210
FT /note="Putative protein-lysine deacylase ABHD14B"
FT /id="PRO_0000361279"
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; 22455 MW; AC4257C81BECDBFB CRC64;
MAGVEQREGA IQVQGQSLFF REALPGGGQA ARFSVLLLHG IRFSSETWQN LGTLHRLAQA
GYRAVAIDLP GLGRSKEAKA PAPIGELVPS SFLAAVVDAL DLGPPVVISP SLSGMYSLPF
LTAPGSQLRG YVPVAPICTD KINAADYARV KASVLIVYGD QDPMGQTSFE HLKQLPNHRV
LVMEGAGHPC YLDKPEEWHT GLLDFLQGLA
