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 17-FEB-2016, entry version 88. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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; Positions=361; Note=Translated as Glu.; 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; CAM16018.1; -; Genomic_DNA. DR CCDS; CCDS51366.1; -. DR RefSeq; NP_941064.2; NM_198662.3. DR UniGene; Mm.184290; -. DR ProteinModelPortal; Q8BM81; -. DR SMR; Q8BM81; 95-383. DR STRING; 10090.ENSMUSP00000030328; -. DR ESTHER; mouse-adcl4; Hormone-sensitive_lipase_like. DR MEROPS; S09.968; -. DR PaxDb; Q8BM81; -. DR PRIDE; Q8BM81; -. DR Ensembl; ENSMUST00000030328; ENSMUSP00000030328; ENSMUSG00000028593. DR GeneID; 381572; -. DR KEGG; mmu:381572; -. DR UCSC; uc008vrh.1; mouse. DR MGI; MGI:2685880; 9430007A20Rik. DR eggNOG; KOG1515; Eukaryota. DR eggNOG; COG0657; LUCA. DR GeneTree; ENSGT00550000074556; -. DR HOGENOM; HOG000231073; -. DR HOVERGEN; HBG058974; -. DR InParanoid; Q8BM81; -. DR KO; K14351; -. DR OMA; YLETKHA; -. DR OrthoDB; EOG7P8P80; -. DR PhylomeDB; Q8BM81; -. DR TreeFam; TF314978; -. DR NextBio; 402262; -. DR PRO; PR:Q8BM81; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; Q8BM81; -. DR CleanEx; MM_9430007A20RIK; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 2. 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 Complete proteome; Glycoprotein; Hydrolase; Membrane; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 407 Arylacetamide deacetylase-like 4. FT /FTId=PRO_0000265938. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 5 25 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 26 407 Lumenal. {ECO:0000255}. FT MOTIF 119 121 Involved in the stabilization of the FT negatively charged intermediate by the FT formation of the oxyanion hole. FT {ECO:0000250|UniProtKB:Q5NUF3}. FT ACT_SITE 193 193 {ECO:0000250|UniProtKB:Q8BLF1}. FT ACT_SITE 347 347 {ECO:0000250|UniProtKB:Q8BLF1}. FT ACT_SITE 377 377 {ECO:0000250|UniProtKB:Q8BLF1}. FT CARBOHYD 168 168 N-linked (GlcNAc...). {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 //