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Database: UniProt
Entry: A0A0M4ETA3_DROBS
LinkDB: A0A0M4ETA3_DROBS
Original site: A0A0M4ETA3_DROBS 
ID   A0A0M4ETA3_DROBS        Unreviewed;       430 AA.
AC   A0A0M4ETA3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Yp3 {ECO:0000313|EMBL:ALC49702.1};
GN   ORFNames=Dbus_chrXg1558 {ECO:0000313|EMBL:ALC49702.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49702.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC49702.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49702.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR   EMBL; CP012528; ALC49702.1; -; Genomic_DNA.
DR   RefSeq; XP_017850529.1; XM_017995040.1.
DR   AlphaFoldDB; A0A0M4ETA3; -.
DR   GeneID; 108605371; -.
DR   OMA; YMGIDAA; -.
DR   OrthoDB; 3687118at2759; -.
DR   Proteomes; UP000494163; Chromosome x sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   PANTHER; PTHR11610:SF186; LIPASE H-RELATED; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..430
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005793754"
FT   DOMAIN          124..404
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   REGION          158..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  47902 MW;  C38898FA9DEB9084 CRC64;
     MNPLRVLSVV ACLAMAAMAS PTSTANQSLK PMEWLTPREL EAIPAVDELT LDRLESMPLQ
     KGAELLQQVY HLSQINHDVE PNYVPSNIQV YWPQPNGEKI VAPFNEMIQR LKQQQNFGED
     EVTVIVTGLP NTVETVKKAN RKLVAAYMQR YNLQAQQQQA QKYTNDLDDE TKNKNQRSSS
     EEDYNELAKN ANTNTGDIIV IDLGSQLTTF KRYAMLDIEK TGNKIGKWIA QLTSELRLPY
     ETIHMIGQNV GAHVAGAAAN EFTRLTGHKL RRVTGLDPSS IIAKYRNTLI GLARGDAEFV
     DVIHTSVYGM GTPIRSGDVD FYPNGPSTGV PGADNVVEAT MRATRYFAES VRPGNERAFP
     AVPANSLKQY KENDGFGKRA YMGIDAAYDI EGDYMLQVNP KSPFGRNAPA QKQSSYHGMH
     TVWQNEKSFQ
//
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