ID   LIP1_ARTBC              Reviewed;         563 AA.
AC   D4ASH1; D4ASH0;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Secreted lipase ARB07186/07185 {ECO:0000305};
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:P20261};
DE   Flags: Precursor;
GN   ORFNames=ARB_07185, ARB_07186;
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:P20261};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE33720.1; Type=Erroneous gene model prediction; Note=ARB_07185 and ARB_07186 have been merged.; Evidence={ECO:0000305};
CC       Sequence=EFE33721.1; Type=Erroneous gene model prediction; Note=ARB_07185 and ARB_07186 have been merged.; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000008; EFE33721.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; ABSU01000008; EFE33720.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003014623.1; XM_003014577.1.
DR   RefSeq; XP_003014624.1; XM_003014578.1.
DR   AlphaFoldDB; D4ASH1; -.
DR   SMR; D4ASH1; -.
DR   ESTHER; trivh-d4d7k4; Fungal_carboxylesterase_lipase.
DR   EnsemblFungi; EFE33720; EFE33720; ARB_07185.
DR   EnsemblFungi; EFE33721; EFE33721; ARB_07186.
DR   GeneID; 9520411; -.
DR   GeneID; 9521781; -.
DR   KEGG; abe:ARB_07185; -.
DR   KEGG; abe:ARB_07186; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   HOGENOM; CLU_006586_4_1_1; -.
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   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..563
FT                   /note="Secreted lipase ARB07186/07185"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001370716"
FT   ACT_SITE        215
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P20261"
FT   DISULFID        83..101
FT                   /evidence="ECO:0000250|UniProtKB:P20261"
FT   DISULFID        268..281
FT                   /evidence="ECO:0000250|UniProtKB:P20261"
SQ   SEQUENCE   563 AA;  61599 MW;  C11EB1725DCCEB36 CRC64;
     MAKYDFVMLW ILTLTAAIAA ARPMVVDKGR QITYTGLDRN GIEVFLGIPF GHDTGGKNRF
     KPPVAVVPPR GSHINATVYG PICPQELRAG SRGKLVISEN CLNLNIGRPK NMTSHDKLAV
     MVTIYGGGYW VGHNQDPRWH ADNMVKESVA NGRPIIHVAM NYRLGVFGFA QTTALRTERS
     ENAALRDQRL ALEWVRDNIA AFGGDPKRVT IFGQSSGGVS VGMQMLAYGG KQPVPYQQGI
     CQSQVLEPGI TGNFTSTAME LVTDKANCTS GDFNSEAALA CLRELDTETL LAAAIATYQN
     GVDHNIGDIW LPSVDGDFLP DAPSVLVAQR RFAPVTSMMG WCEDDVTRFV YPNITTSKGV
     ADFIASYAPN VSRKNIDTLL KLYPTDEFPE NKTAGLSRDF YRTARIFRDI VMTCEPFLVG
     EHAAAEGADA YFFSWNQTIA PSALGVLHGA DLPYVYANLS AYIPPGSPIR PTASDYELSH
     RASRSWSTFG STKEPSLPGH NTFKGFRKSF SKHNEILVFV AGGPNEGLSN IDDHGPHSVI
     GGQKLRERCA FINSPEMIHE LRF