AB17C_MOUSE
ID AB17C_MOUSE Reviewed; 320 AA.
AC Q8VCV1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17C {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17C {ECO:0000312|MGI:MGI:1917428};
DE EC=3.1.2.22 {ECO:0000269|PubMed:27307232};
GN Name=Abhd17c {ECO:0000312|MGI:MGI:1917428};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27307232; DOI=10.1523/jneurosci.0419-16.2016;
RA Yokoi N., Fukata Y., Sekiya A., Murakami T., Kobayashi K., Fukata M.;
RT "Identification of PSD-95 Depalmitoylating Enzymes.";
RL J. Neurosci. 36:6431-6444(2016).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins. Has depalmitoylating activity towards DLG4/PSD95.
CC {ECO:0000269|PubMed:27307232}.
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:0000269|PubMed:27307232};
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; BC018511; AAH18511.1; -; mRNA.
DR CCDS; CCDS21417.2; -.
DR RefSeq; NP_598483.2; NM_133722.2.
DR AlphaFoldDB; Q8VCV1; -.
DR SMR; Q8VCV1; -.
DR BioGRID; 213904; 2.
DR STRING; 10090.ENSMUSP00000112988; -.
DR ESTHER; mouse-Q8VCV1; ABHD17-depalmitoylase.
DR MEROPS; S09.053; -.
DR iPTMnet; Q8VCV1; -.
DR PhosphoSitePlus; Q8VCV1; -.
DR SwissPalm; Q8VCV1; -.
DR EPD; Q8VCV1; -.
DR MaxQB; Q8VCV1; -.
DR PaxDb; Q8VCV1; -.
DR PeptideAtlas; Q8VCV1; -.
DR PRIDE; Q8VCV1; -.
DR ProteomicsDB; 296432; -.
DR Antibodypedia; 63038; 56 antibodies from 14 providers.
DR DNASU; 70178; -.
DR Ensembl; ENSMUST00000117085; ENSMUSP00000112988; ENSMUSG00000038459.
DR GeneID; 70178; -.
DR KEGG; mmu:70178; -.
DR UCSC; uc009ied.2; mouse.
DR CTD; 58489; -.
DR MGI; MGI:1917428; Abhd17c.
DR VEuPathDB; HostDB:ENSMUSG00000038459; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000159424; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q8VCV1; -.
DR OMA; GSRLNCN; -.
DR OrthoDB; 629316at2759; -.
DR PhylomeDB; Q8VCV1; -.
DR TreeFam; TF314365; -.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 70178; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Abhd17c; mouse.
DR PRO; PR:Q8VCV1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VCV1; protein.
DR Bgee; ENSMUSG00000038459; Expressed in epithelium of small intestine and 259 other tissues.
DR Genevisible; Q8VCV1; MM.
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:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; IMP:UniProtKB.
DR GO; GO:1905668; P:positive regulation of protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Cell projection; Endosome; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..320
FT /note="Alpha/beta hydrolase domain-containing protein 17C"
FT /id="PRO_0000297514"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
SQ SEQUENCE 320 AA; 35098 MW; 756E2E43EF5399A4 CRC64;
MPEPGPRMNG FSLGELCWLF CCPPCPSRIA AKLAFLPPEP TYTVLAPEQR APAPAATPAP
APAAQPAPAE EGAGPGACSL HLSERADWQY SQRELDAVEV FFSRTARDNR LGCMFVRCAP
SSRYTLLFSH GNAVDLGQMC SFYIGLGSRI NCNIFSYDYS GYGVSSGKPS EKNLYADIDA
AWQALRTRYG VSPENIILYG QSIGTVPTVD LASRYECAAV ILHSPLMSGL RVAFPDTRKT
YCFDAFPSID KISKVTSPVL VIHGTEDEVI DFSHGLAMYE RCPRAVEPLW VEGAGHNDIE
LYAQYLERLK QFISHELPNS
