ID   ABHEB_PONAB             Reviewed;         210 AA.
AC   Q5R816;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859939; CAH92094.1; -; mRNA.
DR   AlphaFoldDB; Q5R816; -.
DR   SMR; Q5R816; -.
DR   STRING; 9601.ENSPPYP00000015468; -.
DR   ESTHER; ponab-abheb; CIB-CCG1-interacting-factor-B.
DR   PRIDE; Q5R816; -.
DR   eggNOG; ENOG502QR0B; Eukaryota.
DR   InParanoid; Q5R816; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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   Acetylation; Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96IU4"
FT   CHAIN           2..210
FT                   /note="Putative protein-lysine deacylase ABHD14B"
FT                   /id="PRO_0000065040"
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         2
FT                   /note="N-acetylalanine"
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;  27D702DA72A37178 CRC64;
     MAASVEQRED TIQVQGQALF FREARPGSGQ AHFSVLLLHG IRFSSETWQN LGTLHQLAQA
     GYRAVAIDLP GLGRSKEAAA PAPIGELAPG SFLAAVVDAL ELGPPVVISP SLSGMYSLPF
     LTAPGSQLLG YVPVAPICTD KINAANYASV KTPALIVYGD QDPMGQTSFE HLKQLPNHRV
     LIMKGAGHPC YLDKPEEWHT GLLDFLQGLQ