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Database: UniProt
Entry: W5P0X1_SHEEP
LinkDB: W5P0X1_SHEEP
Original site: W5P0X1_SHEEP 
ID   W5P0X1_SHEEP            Unreviewed;       418 AA.
AC   W5P0X1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Arylacetamide deacetylase {ECO:0000256|ARBA:ARBA00044154};
DE            EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
GN   Name=LOC101115927 {ECO:0000313|Ensembl:ENSOARP00000004070.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000004070.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000004070.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000004070.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000004070.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001024};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004464}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004464}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00010515}.
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DR   EMBL; AMGL01010817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004003293.1; XM_004003244.3.
DR   AlphaFoldDB; W5P0X1; -.
DR   STRING; 9940.ENSOARP00000004070; -.
DR   ESTHER; sheep-w5p0x1; Arylacetamide_deacetylase.
DR   MEROPS; S09.991; -.
DR   PaxDb; 9940-ENSOARP00000004070; -.
DR   Ensembl; ENSOART00000004142.1; ENSOARP00000004070.1; ENSOARG00000003815.1.
DR   GeneID; 101115927; -.
DR   KEGG; oas:101115927; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_12_0_1; -.
DR   OMA; PKHMARW; -.
DR   OrthoDB; 1144477at2759; -.
DR   Proteomes; UP000002356; Chromosome 1.
DR   Bgee; ENSOARG00000003815; Expressed in uterus and 51 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR002168; Lipase_GDXG_HIS_AS.
DR   PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR   PANTHER; PTHR23024:SF222; ARYLACETAMIDE DEACETYLASE; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..280
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          333..394
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
SQ   SEQUENCE   418 AA;  48008 MW;  4F39C6CE698BE4C0 CRC64;
     MKFQHSNISA AKKNVQLENI MGRKTILLLI VGVLGAYYVY TPLPDNIEEP WKLMWVTTCL
     KTMTHLCHFA ELLGISHFMD IARFFMSIQE VPPTSDENVT VMETTFNNVP VRIYLPKRKS
     ETLRRGLFYI HGGGWHMGSA AFFDIDFLSR RTAVILDAVV ISTNYRLAPE HHFPSQFEDV
     YNALKWFLNQ DVLDKYSVDP ERIGISGESA GGNLAAAVTQ QLIDDPDVKI KLKTQSLIYP
     ALQCLDLDLP SYRENSNLGL TKSFVARLWS GYFTTDRSLE KAMFFNQHVP VESSHLFKFV
     NWSSFLPEKF RKGHFYKSPT YGNSKLAKKY PGFLDVRAAP LLADDNRLRN LPLTYVITCQ
     YDILRDDGIM YVTRLQNAGV RVTHNHIEDG FHGALVYRGF KIGYRIEKQY MSWLSENL
//
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