ID   LIP2_ARTBC              Reviewed;         507 AA.
AC   D4AZ78;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Secreted lipase ARB_01498 {ECO:0000305};
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:P32946};
DE   Flags: Precursor;
GN   ORFNames=ARB_01498;
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 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:0000250|UniProtKB:P32946};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000020; EFE31598.1; -; Genomic_DNA.
DR   RefSeq; XP_003012238.1; XM_003012192.1.
DR   AlphaFoldDB; D4AZ78; -.
DR   SMR; D4AZ78; -.
DR   STRING; 663331.D4AZ78; -.
DR   ESTHER; trivh-d4dem7; Fungal_carboxylesterase_lipase.
DR   EnsemblFungi; EFE31598; EFE31598; ARB_01498.
DR   GeneID; 9519806; -.
DR   KEGG; abe:ARB_01498; -.
DR   eggNOG; KOG4389; Eukaryota.
DR   HOGENOM; CLU_006586_10_5_1; -.
DR   OMA; GTTMENE; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase 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; IPR002018; CarbesteraseB.
DR   Pfam; PF00135; COesterase; 1.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..507
FT                   /note="Secreted lipase ARB_01498"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434658"
FT   ACT_SITE        196
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P32946"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   507 AA;  55724 MW;  D0FB359E2F79360C CRC64;
     MFVQLLTYGL VAASTLQGVF ASTKLPILDL PYGRWRAAKY DEAADDGSYG PPCIPGPDAP
     GFEDPSYKRQ QKAAREDCLF LDAYVPGNAL RNRGHRKLPV IVWVYGGGYS LGSKDLAIEE
     GIYDGNSLVQ RAAGNAIVIT FNYRLSALGW LAGTTMENEG LPNAGLHDQR AVFEWVRDYV
     HLLGGDRDKV SAWGESAGGG SILSHITANQ GIVDPLFKRA VVMSPGLDFP IDRKGSVENQ
     FKAFASRAGC AGQGLACLRA ANISQLIEAS YKDLGQIGPT PDGRVLKHVF SVDIAQGNYW
     RHLDSLIISH VYDEGGPFVG NDSTLESLSG FLKSNFPTYA TEAVSTLEDY YHLKAPSNES
     VRAIGSRLIR DAIFTCNIRD ILRKYSKKSY LMQYSPKEAT HGQDVFALWY SPKLWNVSIP
     LFSGYQSYFL SHAITGDPNT LRDRDISPPT IAWPKVGDIN AEKLENTLDV VDTGYKLISD
     NQVLKSTCDL WQKLLLDVTK QGGYLDI