ID   A1751_ARTBC             Reviewed;         387 AA.
AC   D4AZY1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Probable 1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000250|UniProtKB:Q13093};
DE            EC=3.1.1.47 {ECO:0000250|UniProtKB:Q13093};
DE   Flags: Precursor;
GN   ORFNames=ARB_01751;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC         Evidence={ECO:0000250|UniProtKB:Q13093};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {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; ABSU01000022; EFE31356.1; -; Genomic_DNA.
DR   RefSeq; XP_003011996.1; XM_003011950.1.
DR   AlphaFoldDB; D4AZY1; -.
DR   SMR; D4AZY1; -.
DR   STRING; 663331.D4AZY1; -.
DR   EnsemblFungi; EFE31356; EFE31356; ARB_01751.
DR   GeneID; 9519320; -.
DR   KEGG; abe:ARB_01751; -.
DR   eggNOG; KOG3847; Eukaryota.
DR   HOGENOM; CLU_026278_0_0_1; -.
DR   OMA; LMISIWY; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005065; PAF_acetylhydro-like.
DR   PANTHER; PTHR10272; PTHR10272; 2.
DR   Pfam; PF03403; PAF-AH_p_II; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..387
FT                   /note="Probable 1-alkyl-2-acetylglycerophosphocholine
FT                   esterase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434479"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q13093"
FT   ACT_SITE        250
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q13093"
FT   ACT_SITE        313
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q13093"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   387 AA;  42265 MW;  81BE2E7B97AB3B35 CRC64;
     MLVQGTIICA LVANAIASSI PSSFLLPEPS GPFKVQREIL ELTDWSRKDI NSTLPRRLMV
     SRFNPIPEKH CIRTEDVPTF PPASAKLEDA ILQAASGGHW VDGLLAASRI RVCADVKKGY
     QTDSHGDNHG IPILLFSPGG NTTRLVYSSI AQTISSAGYT VITMDHPHDT DIVEFLNGDI
     ITGGEVTFSN PSVLPFWNDV RVQDTVFVLN QALKTSPHAR IGMLGHSFGG SAVLSSMVKD
     GRISAGINFD GGLWGDAVNT GLGGRKKPQP YLQWGAYTHN RHNDTSWETL WKAMERLHPH
     AWKKELGIPA GRHNTFSDFP AIIDAGGVRE VIGKASIDVL VGDIPAARSL EFIKVYVHDF
     FQFSLFGKDE GLLRGPSSKY PEVVFLD