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 27-MAR-2024, entry version 53.
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 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 OrthoDB; 3085104at2759; -.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR PANTHER; PTHR11559; CARBOXYLESTERASE; 1.
DR PANTHER; PTHR11559:SF370; CARBOXYLIC ESTER HYDROLASE-RELATED; 1.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
