ID ADCL4_MOUSE Reviewed; 407 AA. AC Q8BM81; A2A751; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 11-DEC-2019, entry version 111. DE RecName: Full=Arylacetamide deacetylase-like 4; DE EC=3.1.1.-; GN Name=Aadacl4; 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=Embryo; 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). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC28757.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK034567; BAC28757.1; ALT_SEQ; mRNA. DR EMBL; AL606902; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS51366.1; -. DR RefSeq; NP_941064.2; NM_198662.3. DR ESTHER; mouse-adcl4; Arylacetamide_deacetylase. DR MEROPS; S09.968; -. DR PhosphoSitePlus; Q8BM81; -. DR PaxDb; Q8BM81; -. DR PRIDE; Q8BM81; -. DR Ensembl; ENSMUST00000030328; ENSMUSP00000030328; ENSMUSG00000028593. DR GeneID; 381572; -. DR KEGG; mmu:381572; -. DR UCSC; uc008vrh.1; mouse. DR CTD; 381572; -. DR MGI; MGI:2685880; 9430007A20Rik. DR eggNOG; KOG1515; Eukaryota. DR eggNOG; COG0657; LUCA. DR GeneTree; ENSGT00940000157630; -. DR HOGENOM; HOG000231073; -. DR InParanoid; Q8BM81; -. DR KO; K14351; -. DR OMA; LPYYHHP; -. DR OrthoDB; 1263520at2759; -. DR PhylomeDB; Q8BM81; -. DR TreeFam; TF314978; -. DR PRO; PR:Q8BM81; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q8BM81; protein. DR Bgee; ENSMUSG00000028593; Expressed in 11 organ(s), highest expression level in medulla oblongata alar plate mantle layer (mouse). DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central. DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central. DR GO; GO:0009056; P:catabolic process; IBA:GO_Central. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013094; AB_hydrolase_3. DR Pfam; PF07859; Abhydrolase_3; 2. DR SUPFAM; SSF53474; SSF53474; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix. FT CHAIN 1..407 FT /note="Arylacetamide deacetylase-like 4" FT /id="PRO_0000265938" FT TOPO_DOM 1..4 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 5..25 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 26..407 FT /note="Lumenal" FT /evidence="ECO:0000255" FT MOTIF 119..121 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 193 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1" FT ACT_SITE 347 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1" FT ACT_SITE 377 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 407 AA; 46220 MW; 22153AF5490E7CD1 CRC64; MLYLVGFLLA TVCLLVLGVN VWVLIDHFLT IDVPPSIPHP VKFRILHFCF HLTTTWGHIL EKMNICSMPQ FFCFLQDSLS SKENHGVFVK DLRFGTIPVR LFRPKAASSK PRRGILFFHG GGAMIGSLDS HHNLCTFLAR ETDSVLVSVG YRKLPYYHHP SLYHDCINAS IHFLKSLKAY GIDPSRVVIC GESIGGAAAV VVTQTLLSRT DIPKIRAQVL IYPILQAFYF QSPSHLMHKN IPFLTKDFMI TCICKYLAID FSWKDAMLTG ACISPSAWKK YEKWLSPDNI PKRFRTTYQP PESPAPFNEA AYLETKHAMN IDISPLVADD KIIAQLPEAF LVSLHWDIIR DDVLLYKKRL EDQGVPVTWH HVEDGFHGCI LLFDKKLFSF PCSLNIVNAV VSYIKDL //