ID   AB17A_BOVIN             Reviewed;         310 AA.
AC   Q2HJ19;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Alpha/beta hydrolase domain-containing protein 17A {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 17A {ECO:0000250|UniProtKB:Q96GS6};
DE            EC=3.1.2.22 {ECO:0000250|UniProtKB:Q96GS6};
GN   Name=ABHD17A {ECO:0000250|UniProtKB:Q96GS6};
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC       proteins. Has depalmitoylating activity towards NRAS. Has
CC       depalmitoylating activity towards DLG4/PSD95. May have depalmitoylating
CC       activity towards MAP6. {ECO:0000250|UniProtKB:Q5XIJ5,
CC       ECO:0000250|UniProtKB:Q96GS6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC         hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:74151; EC=3.1.2.22;
CC         Evidence={ECO:0000250|UniProtKB:Q96GS6};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96GS6};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q96GS6}. Endosome membrane
CC       {ECO:0000250|UniProtKB:Q96GS6}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q96GS6}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:Q5XIJ5}. Postsynaptic density membrane
CC       {ECO:0000250|UniProtKB:Q5XIJ5}.
CC   -!- PTM: Palmitoylated on cysteine residues located in a cysteine cluster
CC       at the N-terminus which promotes membrane localization. Palmitoylation
CC       is required for post-synaptic localization and for depalmitoylating
CC       activity towards DLG4/PSD95. {ECO:0000250|UniProtKB:Q7M759}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC113352; AAI13353.1; -; mRNA.
DR   RefSeq; NP_001040001.1; NM_001046536.1.
DR   AlphaFoldDB; Q2HJ19; -.
DR   SMR; Q2HJ19; -.
DR   STRING; 9913.ENSBTAP00000035338; -.
DR   ESTHER; bovin-AB17A; ABHD17-depalmitoylase.
DR   PaxDb; Q2HJ19; -.
DR   PRIDE; Q2HJ19; -.
DR   GeneID; 614425; -.
DR   KEGG; bta:614425; -.
DR   CTD; 81926; -.
DR   eggNOG; KOG1552; Eukaryota.
DR   InParanoid; Q2HJ19; -.
DR   OrthoDB; 691954at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Endosome; Hydrolase; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW   Synapse.
FT   CHAIN           1..310
FT                   /note="Alpha/beta hydrolase domain-containing protein 17A"
FT                   /id="PRO_0000297508"
FT   ACT_SITE        190
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT   ACT_SITE        255
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   ACT_SITE        284
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GS6"
SQ   SEQUENCE   310 AA;  34102 MW;  63C81CDBF14ECDCC CRC64;
     MNGLSVTELC CLFCCPPCPG RIAAKLAFLP PEPTYSLVPE PEPGPGGAGA APSGNLRALA
     GTPGRWKLHL MERADFQYSQ RELDTIEVFL TKSSRGNRIS CMYVRCVPGA RYTVFFSHGN
     AVDLGQMSSF YIGLGTRINC NIFSYDYSGY GVSSGKPSEK NLYADIDAAW QALRTRYGIS
     PDSIVLYGQS IGTVPTVDLA SRYECAAVVL HSPLTSGMRV AFPDTKKTYC FDAFPNIEKV
     SKITSPVLII HGTEDEVIDF SHGLALYERC PKAVEPLWVE GAGHNDIELY SQYLERLRRF
     ISQELPSQRA