AB17A_RAT
ID AB17A_RAT Reviewed; 310 AA.
AC Q5XIJ5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17A {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17A {ECO:0000312|RGD:1359682};
DE EC=3.1.2.22 {ECO:0000269|PubMed:27307232};
GN Name=Abhd17a {ECO:0000312|RGD:1359682};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [3]
RP FUNCTION.
RX PubMed=28521134; DOI=10.1016/j.neuron.2017.04.042;
RA Tortosa E., Adolfs Y., Fukata M., Pasterkamp R.J., Kapitein L.C.,
RA Hoogenraad C.C.;
RT "Dynamic palmitoylation targets MAP6 to the axon to promote microtubule
RT stabilization during neuronal polarization.";
RL Neuron 94:809-825(2017).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins (PubMed:27307232). Has depalmitoylating activity towards NRAS
CC (By similarity). Has depalmitoylating activity towards DLG4/PSD95
CC (PubMed:27307232). May have depalmitoylating activity towards MAP6
CC (PubMed:28521134). {ECO:0000250|UniProtKB:Q96GS6,
CC ECO:0000269|PubMed:27307232, ECO:0000305|PubMed:28521134}.
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: Cell membrane {ECO:0000269|PubMed:27307232};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GS6}. Recycling endosome membrane
CC {ECO:0000269|PubMed:27307232}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GS6}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:27307232}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:27307232}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in
CC hippocampal neurons. {ECO:0000269|PubMed:27307232}.
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; BC083686; AAH83686.1; -; mRNA.
DR RefSeq; NP_001006984.1; NM_001006983.1.
DR RefSeq; XP_008763312.1; XM_008765090.2.
DR AlphaFoldDB; Q5XIJ5; -.
DR SMR; Q5XIJ5; -.
DR BioGRID; 256279; 1.
DR STRING; 10116.ENSRNOP00000024576; -.
DR ESTHER; ratno-q5xij5; ABHD17-depalmitoylase.
DR PhosphoSitePlus; Q5XIJ5; -.
DR PaxDb; Q5XIJ5; -.
DR Ensembl; ENSRNOT00000024576; ENSRNOP00000024576; ENSRNOG00000018212.
DR GeneID; 299617; -.
DR KEGG; rno:299617; -.
DR UCSC; RGD:1359682; rat.
DR CTD; 81926; -.
DR RGD; 1359682; Abhd17a.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000155854; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q5XIJ5; -.
DR OMA; NDIVCMY; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q5XIJ5; -.
DR TreeFam; TF314365; -.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:Q5XIJ5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000018212; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q5XIJ5; RN.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099033; C:anchored component of postsynaptic recycling endosome membrane; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
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:0072657; P:protein localization to membrane; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
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; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Synapse.
FT CHAIN 1..310
FT /note="Alpha/beta hydrolase domain-containing protein 17A"
FT /id="PRO_0000297511"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 33994 MW; 3937DECDDEEF51F9 CRC64;
MNGLSVSELC CLFCCPPCPG RIAAKLAFLP PEPTYSLVPE PEPGPGGAGA APSGPLRTSA
ATPGRWKIHL TERADFQYGQ RELDTIEVFV TKSARANRIA CMYVRCVPGA RYTVLFSHGN
AVDLGQMCSF YVGLGTRIGC NIFSYDYSGY GISSGRPSEK NLYADIDAAW QALRTRYGIS
PDSIILYGQS IGTVPTVDLA SRYECAAVVL HSPLTSGMRV AFPDTKKTYC FDAFPNIEKV
SKITSPVLII HGTEDEVIDF SHGLALYERC PKAVEPLWVE GAGHNDIELY SQYLERLRRF
ISQELPSQRT
