ID   AB17C_HUMAN             Reviewed;         329 AA.
AC   Q6PCB6; Q1RMD6; Q9NPM1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   02-SEP-2026, entry version 150.
DE   RecName: Full=Alpha/beta hydrolase domain-containing protein 17C {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 17C {ECO:0000312|HGNC:HGNC:26925};
DE            EC=3.1.2.22 {ECO:0000269|PubMed:26701913};
GN   Name=ABHD17C {ECO:0000312|HGNC:HGNC:26925}; Synonyms=FAM108C1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryonic stem cell, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-329.
RG   The European IMAGE consortium;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=26701913; DOI=10.7554/elife.11306;
RA   Lin D.T., Conibear E.;
RT   "ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras
RT   palmitate turnover and subcellular localization.";
RL   Elife 4:E11306-E11306(2015).
CC   -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC       proteins. Has depalmitoylating activity towards NRAS and DLG4/PSD95.
CC       {ECO:0000269|PubMed:26701913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-hexadecanoyl-L-cysteinyl-[protein] + H2O = L-cysteinyl-
CC         [protein] + hexadecanoate + H(+); Xref=Rhea:RHEA:19233, Rhea:RHEA-
CC         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:0000269|PubMed:26701913};
CC   -!- ACTIVITY REGULATION: Inhibited by palmostatin-B.
CC       {ECO:0000269|PubMed:26701913}.
CC   -!- INTERACTION:
CC       Q6PCB6; P01023: A2M; NbExp=3; IntAct=EBI-22011868, EBI-640741;
CC       Q6PCB6; Q92870-2: APBB2; NbExp=3; IntAct=EBI-22011868, EBI-21535880;
CC       Q6PCB6; P54252: ATXN3; NbExp=3; IntAct=EBI-22011868, EBI-946046;
CC       Q6PCB6; P50570-2: DNM2; NbExp=3; IntAct=EBI-22011868, EBI-10968534;
CC       Q6PCB6; P42858: HTT; NbExp=21; IntAct=EBI-22011868, EBI-466029;
CC       Q6PCB6; P51608: MECP2; NbExp=3; IntAct=EBI-22011868, EBI-1189067;
CC       Q6PCB6; Q96CV9: OPTN; NbExp=3; IntAct=EBI-22011868, EBI-748974;
CC       Q6PCB6; Q7Z412: PEX26; NbExp=3; IntAct=EBI-22011868, EBI-752057;
CC       Q6PCB6; O14832: PHYH; NbExp=3; IntAct=EBI-22011868, EBI-721853;
CC       Q6PCB6; A0A6Q8PF08: PMP22; NbExp=3; IntAct=EBI-22011868, EBI-50433196;
CC       Q6PCB6; Q16637: SMN2; NbExp=3; IntAct=EBI-22011868, EBI-395421;
CC       Q6PCB6; P37840: SNCA; NbExp=3; IntAct=EBI-22011868, EBI-985879;
CC       Q6PCB6; O14656: TOR1A; NbExp=3; IntAct=EBI-22011868, EBI-524257;
CC       Q6PCB6; O14656-2: TOR1A; NbExp=3; IntAct=EBI-22011868, EBI-25847109;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PCB6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PCB6-2; Sequence=VSP_027273;
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; BC059401; AAH59401.2; -; mRNA.
DR   EMBL; BC115003; AAI15004.1; -; mRNA.
DR   EMBL; AL390079; CAB98203.1; -; mRNA.
DR   CCDS; CCDS45323.1; -. [Q6PCB6-1]
DR   RefSeq; NP_067037.1; NM_021214.2. [Q6PCB6-1]
DR   AlphaFoldDB; Q6PCB6; -.
DR   SMR; Q6PCB6; -.
DR   BioGRID; 121819; 13.
DR   FunCoup; Q6PCB6; 159.
DR   IntAct; Q6PCB6; 18.
DR   STRING; 9606.ENSP00000258884; -.
DR   ESTHER; human-ABHD17C; ABHD17-depalmitoylase.
DR   MEROPS; S09.053; -.
DR   iPTMnet; Q6PCB6; -.
DR   PhosphoSitePlus; Q6PCB6; -.
DR   SwissPalm; Q6PCB6; -.
DR   BioMuta; ABHD17C; -.
DR   DMDM; 156630444; -.
DR   jPOST; Q6PCB6; -.
DR   MassIVE; Q6PCB6; -.
DR   PaxDb; 9606-ENSP00000258884; -.
DR   PeptideAtlas; Q6PCB6; -.
DR   ProteomicsDB; 67058; -. [Q6PCB6-1]
DR   ProteomicsDB; 67059; -. [Q6PCB6-2]
DR   Pumba; Q6PCB6; -.
DR   Antibodypedia; 63038; 57 antibodies from 15 providers.
DR   DNASU; 58489; -.
DR   Ensembl; ENST00000258884.5; ENSP00000258884.4; ENSG00000136379.13. [Q6PCB6-1]
DR   Ensembl; ENST00000558464.1; ENSP00000452778.1; ENSG00000136379.13. [Q6PCB6-2]
DR   GeneID; 58489; -.
DR   KEGG; hsa:58489; -.
DR   MANE-Select; ENST00000258884.5; ENSP00000258884.4; NM_021214.2; NP_067037.1.
DR   UCSC; uc002bfu.4; human. [Q6PCB6-1]
DR   AGR; HGNC:26925; -.
DR   ClinPGx; PA162385639; -.
DR   CTD; 58489; -.
DR   DisGeNET; 58489; -.
DR   GeneCards; ABHD17C; -.
DR   HGNC; HGNC:26925; ABHD17C.
DR   HPA; ENSG00000136379; Tissue enhanced (intestine).
DR   MIM; 617944; gene.
DR   OpenTargets; ENSG00000136379; -.
DR   VEuPathDB; HostDB:ENSG00000136379; -.
DR   eggNOG; KOG1552; Eukaryota.
DR   GeneTree; ENSGT00940000159424; -.
DR   HOGENOM; CLU_029375_5_4_1; -.
DR   InParanoid; Q6PCB6; -.
DR   OMA; YSEREKX; -.
DR   OrthoDB; 446723at2759; -.
DR   PAN-GO; Q6PCB6; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6PCB6; -.
DR   PathwayCommons; Q6PCB6; -.
DR   Reactome; R-HSA-9648002; RAS processing.
DR   SignaLink; Q6PCB6; -.
DR   Agora; ENSG00000136379; -.
DR   BioGRID-ORCS; 58489; 11 hits in 1144 CRISPR screens.
DR   ChiTaRS; ABHD17C; human.
DR   GenomeRNAi; 58489; -.
DR   Pharos; Q6PCB6; Tbio.
DR   PRO; PR:Q6PCB6; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q6PCB6; protein.
DR   Bgee; ENSG00000136379; Expressed in ileal mucosa and 145 other cell types or tissues.
DR   ExpressionAtlas; Q6PCB6; baseline and differential.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IMP:UniProtKB.
DR   GO; GO:1902817; P:negative regulation of protein localization to microtubule; IBA:GO_Central.
DR   GO; GO:1905668; P:positive regulation of protein localization to endosome; IBA:GO_Central.
DR   GO; GO:0002084; P:protein depalmitoylation; IMP:UniProtKB.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IBA:GO_Central.
DR   FunFam; 3.40.50.1820:FF:000008; Alpha/beta hydrolase domain-containing protein 17B; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR022742; ABHD17C-like.
DR   PANTHER; PTHR12277; ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12277:SF55; ALPHA_BETA HYDROLASE DOMAIN-CONTAINING PROTEIN 17C; 1.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Endosome; Hydrolase;
KW   Lipoprotein; Membrane; Palmitate; Postsynaptic cell membrane;
KW   Proteomics identification; Reference proteome; Synapse.
FT   CHAIN           1..329
FT                   /note="Alpha/beta hydrolase domain-containing protein 17C"
FT                   /id="PRO_0000297513"
FT   REGION          53..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Low complexity"
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"
FT   VAR_SEQ         223..256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027273"
SQ   SEQUENCE   329 AA;  35831 MW;  A5EE8ED4291EC49F CRC64;
     MPEPGPRMNG FSLGELCWLF CCPPCPSRIA AKLAFLPPEP TYTVLAPEQR GAGASAPAPA
     QATAAAAAAQ PAPQQPEEGA 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
//