ID   LIP3_ARTBC              Reviewed;         564 AA.
AC   D4B1N9;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Probable secreted lipase ARB_02369 {ECO:0000305};
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:P20261};
DE   Flags: Precursor;
GN   ORFNames=ARB_02369;
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], IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
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:21247460,
CC       ECO:0000269|PubMed:21919205}.
CC   -!- INDUCTION: Expression is down-regulated in presence of human
CC       keratinocytes. {ECO:0000269|PubMed:21247460}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000027; EFE30671.1; -; Genomic_DNA.
DR   RefSeq; XP_003011311.1; XM_003011265.1.
DR   AlphaFoldDB; D4B1N9; -.
DR   SMR; D4B1N9; -.
DR   STRING; 663331.D4B1N9; -.
DR   ESTHER; trivh-d4d500; Fungal_carboxylesterase_lipase.
DR   EnsemblFungi; EFE30671; EFE30671; ARB_02369.
DR   GeneID; 9524050; -.
DR   KEGG; abe:ARB_02369; -.
DR   eggNOG; KOG4389; Eukaryota.
DR   HOGENOM; CLU_006586_10_6_1; -.
DR   OMA; TNAGEDC; -.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; Glycoprotein; Hydrolase; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..564
FT                   /note="Probable secreted lipase ARB_02369"
FT                   /id="PRO_5001370717"
FT   ACT_SITE        235
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        89..123
FT                   /evidence="ECO:0000250|UniProtKB:P20261"
SQ   SEQUENCE   564 AA;  61385 MW;  B7257A09261C4A9E CRC64;
     MWSLLTAAVL FARLSIAVPT TAAPAIEKRA APTVQLDYAT VVGSSALGID SFKGIPYAQP
     PVGKLRLKPP QPITGDLGTV QATGLPRACP QMYLKSDDIP DDILGRFINT PVFQKITHAG
     EDCLTINVQK PSSATPESKL PVLFWIFGGG FEFGSTQLYD GTSLILRSMA QNRDIIFVAV
     NYRVGGFGFL PGADIKKDGS ANLGLLDQRL GLQWVAENIE KFGGDPEKVT IWGESAGAIS
     VFDQMALYDG DNTYKGKPLF RGAIMNSGSV IPADPVDCPK GEVVYEKVVE EAGCSKATDK
     LDCLRSVDYT TFLNAANSVP GILSYNSVAL SYLPRPDGKA LTASPDKLGR SGLLAKVPLI
     IGDQEDEGTL FSLVQNNITT TEHLVDYFST YFFHGATKEQ LRALVDTYPN DPSAGSPFRT
     GNLNQLYPQY KRLAAMLGDL VFTLSRRVFL DIANSKFPEI PTYSYLGTYG HIIPILGTSH
     GSDVLTSFGY TPGIPSTSIQ NYYLSFVNNL DPNKGTPLGF PKWPRWSEGK MLLNFEAVKN
     SLLKDDFRGE SAKYLEEHTD ILHI