ID   AB17C_CHICK             Reviewed;         310 AA.
AC   Q5ZJX1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; ORFNames=RCJMB04_14o5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC       proteins. Has depalmitoylating activity towards NRAS.
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.
CC       {ECO:0000250|UniProtKB:Q7M759}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ720313; CAG31972.1; -; mRNA.
DR   RefSeq; NP_001007827.1; NM_001007826.1.
DR   AlphaFoldDB; Q5ZJX1; -.
DR   SMR; Q5ZJX1; -.
DR   STRING; 9031.ENSGALP00000010347; -.
DR   MEROPS; S09.053; -.
DR   PaxDb; Q5ZJX1; -.
DR   Ensembl; ENSGALT00000010361; ENSGALP00000010347; ENSGALG00000006420.
DR   GeneID; 415479; -.
DR   KEGG; gga:415479; -.
DR   CTD; 58489; -.
DR   VEuPathDB; HostDB:geneid_415479; -.
DR   eggNOG; KOG1552; Eukaryota.
DR   GeneTree; ENSGT00940000159424; -.
DR   HOGENOM; CLU_029375_5_4_1; -.
DR   InParanoid; Q5ZJX1; -.
DR   OMA; GSRLNCN; -.
DR   OrthoDB; 629316at2759; -.
DR   PhylomeDB; Q5ZJX1; -.
DR   TreeFam; TF314365; -.
DR   Reactome; R-GGA-9648002; RAS processing.
DR   PRO; PR:Q5ZJX1; -.
DR   Proteomes; UP000000539; Chromosome 10.
DR   Bgee; ENSGALG00000006420; Expressed in spermatocyte and 12 other tissues.
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..310
FT                   /note="Alpha/beta hydrolase domain-containing protein 17C"
FT                   /id="PRO_0000297515"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   ACT_SITE        286
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
SQ   SEQUENCE   310 AA;  34238 MW;  213E82C96A047368 CRC64;
     MPEQGPRMNG FSLGELCWLF CCPPCPSRIA AKLAFLPPEP TYTVLPPEQQ QEAGAASGAA
     TPTGSGTCSL HLSERADWQY SQRELDAVEV FFSRTARDNR LGCMFVRCAP TGRYTLLFSH
     GNAVDLGQMC SFYIGLGSRI NCNVFSYDYS GYGVSTGKPS EKNLYADIDA AWQALRTRYG
     VSPENIILYG QSIGTVPTVD LASRYECAAV ILHSPLMSGL RVAFPDTRKT YCFDAFPSID
     KISKVTSPVL VIHGTEDEVI DFSHGLAMYE RCPRAVEPLW VEGAGHNDIE LYAQYLERLK
     QFISHELPNS