ID   ADCL3_MOUSE             Reviewed;         408 AA.
AC   A2A7Z8;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Arylacetamide deacetylase-like 3;
DE            EC=3.1.1.-;
GN   Name=Aadacl3;
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 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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL607073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS38954.1; -.
DR   RefSeq; NP_001078972.1; NM_001085503.2.
DR   AlphaFoldDB; A2A7Z8; -.
DR   SMR; A2A7Z8; -.
DR   STRING; 10090.ENSMUSP00000101375; -.
DR   ESTHER; mouse-adcl3; Arylacetamide_deacetylase.
DR   GlyGen; A2A7Z8; 1 site.
DR   iPTMnet; A2A7Z8; -.
DR   PhosphoSitePlus; A2A7Z8; -.
DR   PaxDb; A2A7Z8; -.
DR   PRIDE; A2A7Z8; -.
DR   ProteomicsDB; 285681; -.
DR   Antibodypedia; 57582; 48 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000105749; ENSMUSP00000101375; ENSMUSG00000078507.
DR   GeneID; 230883; -.
DR   KEGG; mmu:230883; -.
DR   UCSC; uc008vrg.1; mouse.
DR   CTD; 126767; -.
DR   MGI; MGI:2685281; Aadacl3.
DR   VEuPathDB; HostDB:ENSMUSG00000078507; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   GeneTree; ENSGT00940000162160; -.
DR   HOGENOM; CLU_012494_12_2_1; -.
DR   InParanoid; A2A7Z8; -.
DR   OMA; TCIVSCE; -.
DR   OrthoDB; 1263520at2759; -.
DR   PhylomeDB; A2A7Z8; -.
DR   TreeFam; TF314978; -.
DR   BioGRID-ORCS; 230883; 2 hits in 73 CRISPR screens.
DR   PRO; PR:A2A7Z8; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2A7Z8; protein.
DR   Bgee; ENSMUSG00000078507; Expressed in lip and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR017157; Arylacetamide_deacetylase.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..408
FT                   /note="Arylacetamide deacetylase-like 3"
FT                   /id="PRO_0000389253"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           120..122
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  46340 MW;  948C83A1E308C4B7 CRC64;
     MVVLALTLLV GSVAVFSLGS LLWVVGKHFW TEHIPEGITH PWRLRILSCL FHLTMTWGMI
     FEKLGLCYAP QFASFLHDLK PLKRDPDVVV KDLHFGTIPV KLYKPKKPSS IPRLGIIFFH
     GGGTIIGSLR THNSICLRLS KECDSVVVSV GYRKSPMYKY PVMKDDCVVA TTHFLESLDV
     YGVDPARVVT CGDSVGGTAA TVTSQMLVHR PDLPRIKAQI LIYPLLQLID FGSPSYQQNR
     NIPLLSWDLA FYCFCCHLDV NISWKSVVKN GMHLPPDVWE KYRKWLGAEN IPERFKNRGY
     KSIPWGPVNN DAYQEIKRSL NYTCSPLISE DSIVSQLPET CIVSCEYDLL RDHSLLYKKR
     LEDLGVPVTW HHMEDGFHGV LSALDYGLLS FPCASRIMDL IIQFIRKF