ADCL2_HUMAN
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 03-AUG-2022, entry version 128.
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};
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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 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; Q6P093; -.
DR PeptideAtlas; Q6P093; -.
DR PRIDE; Q6P093; -.
DR ProteomicsDB; 66809; -. [Q6P093-1]
DR Antibodypedia; 33616; 124 antibodies from 14 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 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; WKVMALD; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q6P093; -.
DR TreeFam; TF314978; -.
DR PathwayCommons; Q6P093; -.
DR SABIO-RK; Q6P093; -.
DR BioGRID-ORCS; 344752; 13 hits in 1072 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 tissues.
DR ExpressionAtlas; Q6P093; baseline and differential.
DR Genevisible; Q6P093; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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 InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
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
