ID   AB17C_BOVIN             Reviewed;         329 AA.
AC   A5PKD9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Alpha/beta hydrolase domain-containing protein 17C {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 17C {ECO:0000250|UniProtKB:Q6PCB6};
DE            EC=3.1.2.22 {ECO:0000250|UniProtKB:Q8VCV1};
GN   Name=ABHD17C {ECO:0000250|UniProtKB:Q6PCB6};
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=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC       proteins. Has depalmitoylating activity towards NRAS and DLG4/PSD95.
CC       {ECO:0000250|UniProtKB:Q6PCB6}.
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:Q6PCB6};
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:B5DFK7}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:B5DFK7}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:B5DFK7}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:B5DFK7}. Postsynaptic density membrane
CC       {ECO:0000250|UniProtKB:B5DFK7}.
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}.
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DR   EMBL; BC142452; AAI42453.1; -; mRNA.
DR   RefSeq; NP_001092484.1; NM_001099014.1.
DR   AlphaFoldDB; A5PKD9; -.
DR   SMR; A5PKD9; -.
DR   STRING; 9913.ENSBTAP00000044044; -.
DR   ESTHER; bovin-AB17C; ABHD17-depalmitoylase.
DR   PaxDb; A5PKD9; -.
DR   PRIDE; A5PKD9; -.
DR   Ensembl; ENSBTAT00000046785; ENSBTAP00000044044; ENSBTAG00000032951.
DR   GeneID; 520956; -.
DR   KEGG; bta:520956; -.
DR   CTD; 58489; -.
DR   VEuPathDB; HostDB:ENSBTAG00000032951; -.
DR   VGNC; VGNC:53931; ABHD17C.
DR   eggNOG; KOG1552; Eukaryota.
DR   GeneTree; ENSGT00940000159424; -.
DR   HOGENOM; CLU_029375_5_4_1; -.
DR   InParanoid; A5PKD9; -.
DR   OMA; GSRLNCN; -.
DR   OrthoDB; 629316at2759; -.
DR   TreeFam; TF314365; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000032951; Expressed in rumen papilla and 101 other tissues.
DR   ExpressionAtlas; A5PKD9; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR   GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IBA:GO_Central.
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; Postsynaptic cell membrane; Reference proteome; Synapse.
FT   CHAIN           1..329
FT                   /note="Alpha/beta hydrolase domain-containing protein 17C"
FT                   /id="PRO_0000297512"
FT   REGION          46..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT   ACT_SITE        276
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
SQ   SEQUENCE   329 AA;  35864 MW;  AEA592D2ABD1DFEF CRC64;
     MPEPGPRMNG FSLGELCWLF CCPPCPSRIA AKLAFLPPEP TYTVLAPEQR GPGAPAPASA
     ASTSSASAAA QPAPQQPEEG GAGPGACSLH LSERADWQYS QRELDAVEVF FSRTARDNRL
     GCMFVRCAPS SRYTLLFSHG NAVDLGQMCS FYIGLGSRIN CNIFSYDYSG YGVSSGKPSE
     KNLYADIDAA WQALRTRYGV SPENIILYGQ SIGTVPTVDL ASRYECAAVI LHSPLMSGLR
     VAFPDTRKTY CFDAFPSIDK ISKVTSPVLV IHGTEDEVID FSHGLAMYER CPRAVEPLWV
     EGAGHNDIEL YAQYLERLKQ FISHELPNS