AB17B_RAT
ID AB17B_RAT Reviewed; 288 AA.
AC Q6AY17;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17B {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17B {ECO:0000312|RGD:1305246};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:Q5VST6};
GN Name=Abhd17b {ECO:0000312|RGD:1305246};
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=Testis;
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 PROTEIN SEQUENCE OF 200-206, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP 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).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins. Has depalmitoylating activity towards DLG4/PSD95. Has
CC depalmitoylating activity towards GAP43. Has depalmitoylating activity
CC towards MAP6. Has depalmitoylating activity towards NRAS.
CC {ECO:0000250|UniProtKB:Q5VST6, ECO:0000250|UniProtKB:Q7M759}.
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:Q7M759};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27307232};
CC Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side
CC {ECO:0000269|PubMed:27307232}. Recycling endosome membrane
CC {ECO:0000269|PubMed:27307232}; Lipid-anchor
CC {ECO:0000269|PubMed:27307232}; Cytoplasmic side
CC {ECO:0000269|PubMed:27307232}. 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).
CC {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; BC079229; AAH79229.1; -; mRNA.
DR RefSeq; NP_001014050.1; NM_001014028.1.
DR RefSeq; XP_006231224.1; XM_006231162.3.
DR AlphaFoldDB; Q6AY17; -.
DR SMR; Q6AY17; -.
DR STRING; 10116.ENSRNOP00000047508; -.
DR ESTHER; ratno-q6ay17; ABHD17-depalmitoylase.
DR MEROPS; S09.055; -.
DR iPTMnet; Q6AY17; -.
DR PhosphoSitePlus; Q6AY17; -.
DR SwissPalm; Q6AY17; -.
DR PaxDb; Q6AY17; -.
DR PRIDE; Q6AY17; -.
DR Ensembl; ENSRNOT00000044486; ENSRNOP00000047508; ENSRNOG00000012514.
DR GeneID; 309399; -.
DR KEGG; rno:309399; -.
DR UCSC; RGD:1305246; rat.
DR CTD; 51104; -.
DR RGD; 1305246; Abhd17b.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000157611; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q6AY17; -.
DR OMA; FMTRTCK; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q6AY17; -.
DR TreeFam; TF314365; -.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:Q6AY17; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012514; Expressed in testis and 19 other tissues.
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; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISO:RGD.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; ISO:RGD.
DR GO; GO:1905668; P:positive regulation of protein localization to endosome; ISO:RGD.
DR GO; GO:0002084; P:protein depalmitoylation; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:1902473; P:regulation of protein localization to synapse; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing; Endosome;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..288
FT /note="Alpha/beta hydrolase domain-containing protein 17B"
FT /id="PRO_0000281113"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 288 AA; 32201 MW; 4A797F710C99EC72 CRC64;
MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLMCD ESGSRWTLHL SERADWQYSS
REKDAIECFM TRTSKGNRIA CMFVRCSPNA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
NIFSYDYSGY GASSGKPTEK NLYADVEAAW LALRTRYGIR PENVIIYGQS IGTVPSVDLA
ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKQF VSQELVNL
