AB17B_MOUSE
ID AB17B_MOUSE Reviewed; 288 AA.
AC Q7M759; Q58EV9; Q8K275;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17B {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17B {ECO:0000312|MGI:MGI:1917816};
DE EC=3.1.2.22 {ECO:0000269|PubMed:27307232, ECO:0000305|PubMed:28521134};
GN Name=Abhd17b {ECO:0000312|MGI:MGI:1917816};
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 STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-288.
RC STRAIN=Czech II, and FVB/N-3; 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 [4]
RP IDENTIFICATION.
RC STRAIN=C57BL/6J;
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PALMITOYLATION, ACTIVE SITE, AND MUTAGENESIS OF 1-MET--GLY-20;
RP 10-CYS--CYS-18; SER-170; ASP-235 AND HIS-264.
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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
CC DLG4/PSD95 (PubMed:27307232). Has depalmitoylating activity towards
CC GAP43 (PubMed:27307232). Has depalmitoylating activity towards MAP6
CC (PubMed:28521134). Has depalmitoylating activity towards NRAS (By
CC similarity). {ECO:0000250|UniProtKB:Q5VST6,
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, ECO:0000305|PubMed:28521134};
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. {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:0000269|PubMed:27307232}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC {ECO:0000305}.
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DR EMBL; AK152807; BAE31512.1; -; mRNA.
DR EMBL; AC133649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032261; AAH32261.1; -; mRNA.
DR EMBL; BC091733; AAH91733.1; -; mRNA.
DR EMBL; BN000127; CAD67578.1; -; mRNA.
DR CCDS; CCDS29700.1; -.
DR RefSeq; NP_666208.2; NM_146096.3.
DR RefSeq; XP_011245530.1; XM_011247228.2.
DR AlphaFoldDB; Q7M759; -.
DR SMR; Q7M759; -.
DR STRING; 10090.ENSMUSP00000056099; -.
DR ESTHER; mouse-q7m759; ABHD17-depalmitoylase.
DR MEROPS; S09.055; -.
DR iPTMnet; Q7M759; -.
DR PhosphoSitePlus; Q7M759; -.
DR SwissPalm; Q7M759; -.
DR EPD; Q7M759; -.
DR MaxQB; Q7M759; -.
DR PaxDb; Q7M759; -.
DR PeptideAtlas; Q7M759; -.
DR PRIDE; Q7M759; -.
DR ProteomicsDB; 285896; -.
DR Antibodypedia; 26944; 33 antibodies from 15 providers.
DR DNASU; 226016; -.
DR Ensembl; ENSMUST00000052556; ENSMUSP00000056099; ENSMUSG00000047368.
DR GeneID; 226016; -.
DR KEGG; mmu:226016; -.
DR UCSC; uc008gzb.1; mouse.
DR CTD; 51104; -.
DR MGI; MGI:1917816; Abhd17b.
DR VEuPathDB; HostDB:ENSMUSG00000047368; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000157611; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q7M759; -.
DR OMA; FMTRTCK; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q7M759; -.
DR TreeFam; TF314365; -.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 226016; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Abhd17b; mouse.
DR PRO; PR:Q7M759; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q7M759; protein.
DR Bgee; ENSMUSG00000047368; Expressed in dorsal pancreas and 225 other tissues.
DR ExpressionAtlas; Q7M759; baseline and differential.
DR Genevisible; Q7M759; MM.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099033; C:anchored component of postsynaptic recycling endosome membrane; ISO:MGI.
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; 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; IMP:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IMP:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IMP:UniProtKB.
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; Endosome; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Synapse.
FT CHAIN 1..288
FT /note="Alpha/beta hydrolase domain-containing protein 17B"
FT /id="PRO_0000281112"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:27307232"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:27307232"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:27307232"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 1..20
FT /note="MNNLSFSELCCLFCCPPCPG->MGSNKSKPKDASQRRRSLEP: Loss of
FT palmitoylation activity towards LG4/PSD95 and appears more
FT diffused at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:27307232"
FT MUTAGEN 10..18
FT /note="CCLFCCPPC->SSLFSSPPS: Loss of palmitoylation and
FT plasma membrane localization. Loss of LG4/PSD95
FT depalmitoylation."
FT /evidence="ECO:0000269|PubMed:27307232"
FT MUTAGEN 170
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27307232"
FT MUTAGEN 235
FT /note="D->A: Loss of catalytic activity. No effect on its
FT localization. Trapping-mutant that stabilizes interaction
FT with LG4/PSD95."
FT /evidence="ECO:0000269|PubMed:27307232"
FT MUTAGEN 264
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27307232"
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
