ID   LIPA_ARTBC              Reviewed;         469 AA.
AC   D4AX63;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Lipase A {ECO:0000250|UniProtKB:W3VKA4};
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:W3VKA4};
DE   Flags: Precursor;
GN   ORFNames=ARB_00790;
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).
CC   -!- FUNCTION: Hydrolyzes triglycerides, with a preference for substrates
CC       with short-chain lengths (C4 to C8). {ECO:0000250|UniProtKB:W3VKA4}.
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:W3VKA4};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:W3VKA4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:W3VKA4}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000016; EFE32268.1; -; Genomic_DNA.
DR   RefSeq; XP_003012908.1; XM_003012862.1.
DR   AlphaFoldDB; D4AX63; -.
DR   SMR; D4AX63; -.
DR   ESTHER; artbc-d4ax63; Fungal-Bact_LIP.
DR   EnsemblFungi; EFE32268; EFE32268; ARB_00790.
DR   GeneID; 9522986; -.
DR   KEGG; abe:ARB_00790; -.
DR   eggNOG; ENOG502S2P7; Eukaryota.
DR   HOGENOM; CLU_029538_5_0_1; -.
DR   OMA; SAWAAEM; -.
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; IPR005152; Lipase_secreted.
DR   PANTHER; PTHR34853; PTHR34853; 1.
DR   Pfam; PF03583; LIP; 1.
DR   PIRSF; PIRSF029171; Esterase_LipA; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..469
FT                   /note="Lipase A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434478"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT   ACT_SITE        361
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT   ACT_SITE        393
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        129..304
FT                   /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT   DISULFID        377..421
FT                   /evidence="ECO:0000250|UniProtKB:W3VKA4"
SQ   SEQUENCE   469 AA;  50460 MW;  AA5800992D246FC9 CRC64;
     MMFLTQLVSA LFLFFLGPIS YGKPVETFVL PLAQDAPIPP SEDPFYQPPP GYEETEPGTV
     LRQRRPPFPI SLFRSAPIDL AATYQVLYRS SDTFGQPTAT VSTILIPHNA NMSKVLSYQV
     VEDAAFINCA PSYALQLHSD PGGLFGTIII QSELLLITAA LENGWVVTIP DYEGPAAAFL
     AYWRAGYATL DGIRATLASS GFTGVDPDAA VGLWGTSGGS VASAFAADLH PKYAPELNIV
     GAALGGVVPS ITTALHSLNK GFDAGIIVSG VIGLSKEYTY MQPILESYLV PHLRDKFMSA
     GKKCSGAVSL DFRMEDIFSY FKGGEESGLF ADPRVKAILD HNAMPQGVPE IPILILKSVN
     DEISPISDTD ALVEKYCSNG VTIDYKRDLL SVHTILAVTG APEAVLWLRD RLDGITVEKG
     CKTSTIFMTL LQPGALEVMS KTIIDNLLNL LGKPVGPRLR TEIVHVPPL