ID ADCL2_HUMAN Reviewed; 401 AA. AC Q6P093; Q5HYJ4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 24-JAN-2024, entry version 135. DE RecName: Full=Arylacetamide deacetylase-like 2; DE EC=3.1.1.-; DE Flags: Precursor; GN Name=AADACL2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Adipose tissue; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-186. RC TISSUE=Placenta; 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). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6P093-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P093-3; Sequence=VSP_038389, VSP_038390; CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH65724.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAI46075.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; 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; BX647585; CAI46075.1; ALT_SEQ; mRNA. DR EMBL; AC069067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC065724; AAH65724.1; ALT_INIT; mRNA. DR CCDS; CCDS3161.2; -. [Q6P093-1] DR RefSeq; NP_997248.2; NM_207365.3. [Q6P093-1] DR AlphaFoldDB; Q6P093; -. DR SMR; Q6P093; -. DR BioGRID; 131319; 1. DR STRING; 9606.ENSP00000348911; -. DR DrugBank; DB07814; Gibberellic acid. DR DrugBank; DB07815; Gibberellin A4. DR ESTHER; human-AADACL2; Arylacetamide_deacetylase. DR iPTMnet; Q6P093; -. DR PhosphoSitePlus; Q6P093; -. DR BioMuta; AADACL2; -. DR DMDM; 269849709; -. DR jPOST; Q6P093; -. DR MassIVE; Q6P093; -. DR PaxDb; 9606-ENSP00000348911; -. DR PeptideAtlas; Q6P093; -. DR ProteomicsDB; 66809; -. [Q6P093-1] DR Antibodypedia; 33616; 134 antibodies from 15 providers. DR DNASU; 344752; -. DR Ensembl; ENST00000356517.4; ENSP00000348911.3; ENSG00000197953.6. [Q6P093-1] DR Ensembl; ENST00000570799.1; ENSP00000461239.1; ENSG00000261846.2. [Q6P093-1] DR GeneID; 344752; -. DR KEGG; hsa:344752; -. DR MANE-Select; ENST00000356517.4; ENSP00000348911.3; NM_207365.4; NP_997248.2. DR UCSC; uc003ezc.4; human. [Q6P093-1] DR AGR; HGNC:24427; -. DR CTD; 344752; -. DR GeneCards; AADACL2; -. DR HGNC; HGNC:24427; AADACL2. DR HPA; ENSG00000197953; Tissue enriched (skin). DR neXtProt; NX_Q6P093; -. DR OpenTargets; ENSG00000197953; -. DR PharmGKB; PA142670463; -. DR VEuPathDB; HostDB:ENSG00000197953; -. DR eggNOG; KOG1515; Eukaryota. DR GeneTree; ENSGT00940000161405; -. DR HOGENOM; CLU_012494_12_0_1; -. DR InParanoid; Q6P093; -. DR OMA; DHVYTEP; -. DR OrthoDB; 1144477at2759; -. DR PhylomeDB; Q6P093; -. DR TreeFam; TF314978; -. DR PathwayCommons; Q6P093; -. DR SABIO-RK; Q6P093; -. DR BioGRID-ORCS; 344752; 13 hits in 1150 CRISPR screens. DR ChiTaRS; AADACL2; human. DR GenomeRNAi; 344752; -. DR Pharos; Q6P093; Tdark. DR PRO; PR:Q6P093; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q6P093; Protein. DR Bgee; ENSG00000197953; Expressed in skin of abdomen and 40 other cell types or tissues. DR ExpressionAtlas; Q6P093; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013094; AB_hydrolase_3. DR InterPro; IPR017157; Arylacetamide_deacetylase. DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS. DR PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1. DR PANTHER; PTHR23024:SF223; ARYLACETAMIDE DEACETYLASE-LIKE 2; 1. DR Pfam; PF07859; Abhydrolase_3; 2. DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS01174; LIPASE_GDXG_SER; 1. DR Genevisible; Q6P093; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Disulfide bond; Hydrolase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..401 FT /note="Arylacetamide deacetylase-like 2" FT /id="PRO_0000314960" FT MOTIF 111..113 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 189 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1, FT ECO:0000255|PROSITE-ProRule:PRU10038" FT ACT_SITE 341 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1" FT ACT_SITE 371 FT /evidence="ECO:0000250|UniProtKB:Q8BLF1" FT DISULFID 116..338 FT /evidence="ECO:0000250" FT VAR_SEQ 47..53 FT /note="AMCFENM -> NRGPLTS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038389" FT VAR_SEQ 54..401 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038390" FT VARIANT 186 FT /note="A -> S (in dbSNP:rs1972977)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038140" FT VARIANT 343 FT /note="L -> I (in dbSNP:rs1052562)" FT /id="VAR_038141" FT CONFLICT 26 FT /note="N -> S (in Ref. 1; CAI46075)" FT /evidence="ECO:0000305" SQ SEQUENCE 401 AA; 46099 MW; 801AF004D9E6A3DA CRC64; MGLKALCLGL LCVLFVSHFY TPMPDNIEES WKIMALDAIA KTCTFTAMCF ENMRIMRYEE FISMIFRLDY TQPLSDEYIT VTDTTFVDIP VRLYLPKRKS ETRRRAVIYF HGGGFCFGSS KQRAFDFLNR WTANTLDAVV VGVDYRLAPQ HHFPAQFEDG LAAVKFFLLE KILTKYGVDP TRICIAGDSS GGNLATAVTQ QVQNDAEIKH KIKMQVLLYP GLQITDSYLP SHRENEHGIV LTRDVAIKLV SLYFTKDEAL PWAMRRNQHM PLESRHLFKF VNWSILLPEK YRKDYVYTEP ILGGLSYSLP GLTDSRALPL LANDSQLQNL PLTYILTCQH DLLRDDGLMY VTRLRNVGVQ VVHEHIEDGI HGALSFMTSP FYLRLGLRIR DMYVSWLDKN L //