ID A0A2N5VXA2_9BASI Unreviewed; 481 AA.
AC A0A2N5VXA2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=Acyl-protein thioesterase 1 {ECO:0000256|ARBA:ARBA00014923};
DE EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00031195};
GN ORFNames=PCANC_05369 {ECO:0000313|EMBL:PLW54613.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW54613.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW54613.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW54613.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins with a strong preference for palmitoylated G-alpha proteins
CC over other acyl substrates. Mediates the deacylation of G-alpha
CC proteins such as GPA1 in vivo, but has weak or no activity toward
CC palmitoylated Ras proteins. Has weak lysophospholipase activity in
CC vitro; however such activity may not exist in vivo.
CC {ECO:0000256|ARBA:ARBA00029392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000072};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW54613.1}.
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DR EMBL; PGCJ01000043; PLW54613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5VXA2; -.
DR STRING; 200324.A0A2N5VXA2; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10655:SF17; PALMITOYL-PROTEIN HYDROLASE; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..397
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 481 AA; 53167 MW; 8430779B05EFEBCE CRC64;
MNTGDKLNPC ARLLVKVKPV VSSVEALTFK ASFLKRSYHG TDLRSLHLST EKASFKNPLS
DSPYQPTHSF GITLRPPRKT LSFYLCLFLA AAALIVMVCL TVIGFGERSH CLDCANSVSN
HLESVPSTIP PREQFTPSEY RANWTKPTQG VSAVAFDVIP PLDQNNGRGF GWTVFFIHGL
GDYNASASYH WRESLLASYL DPLAGNSFGN LTGLQFIFPK AHVRPVTVYS AQKNQGARPG
WFDIKDWSDL YYLEDEEGLR QSAIGLSTIL KDEALAGRIQ LNQTIIAGFS QGAVMSILLT
LALPQPPAAC IMMSGYLPLP LRLVDLGSSS PAAYKKTSFY WLHGTNDAVL KYNQARSGMK
LFSALFSDKF LRGKFKTFLG LQHGFNADEE KVASNYIDGI VSRNTGGLFD SSFDAYIEPE
NEGDVIQSRL SQVRAVLQHR VLFGTRYPFS EDDQITVLLS QDTGREPPIR TQEGKLLIAT
P
//
