ID A0A131ZWD0_SARSC Unreviewed; 1252 AA.
AC A0A131ZWD0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Lipase-like protein 1 {ECO:0000313|EMBL:KPM03142.1};
GN ORFNames=QR98_0015720 {ECO:0000313|EMBL:KPM03142.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM03142.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM03142.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM03142.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM03142.1}.
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DR EMBL; JXLN01004210; KPM03142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A131ZWD0; -.
DR VEuPathDB; VectorBase:SSCA007674; -.
DR OrthoDB; 3091216at2759; -.
DR Proteomes; UP000616769; Unassembled WGS 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; 3.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF178; FI22312P1; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 2.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 3.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
PE 3: Inferred from homology;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1..329
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT DOMAIN 353..453
FT /note="PLAT"
FT /evidence="ECO:0000259|Pfam:PF01477"
FT DOMAIN 789..1097
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPM03142.1"
SQ SEQUENCE 1252 AA; 141094 MW; 83F4132099059836 CRC64;
SVCYGEYGCF NKTELSNEIK IANLASKLPE SPEEQDVHFY FFSCRNRLNP IRKRFNVEEK
DLRDIGFDPN NQTIVMVHGY TDFYNEFNWM GDLKDSILNT QNCKSNLIIV DWSFGAKAPY
SQAVANTRVV GSIIAVLIQK LNNVYKTSNN DFIILGHSLG GQIVGFAGKR INNPKVRLII
GLDPAGPAFN NVTESNHLTP NDGQLVVTVH TNGAANIVDG LGIDKPLGHY SFFPNGGSVQ
PGCEPAKGVA SVLAKGLGEG VADAFACSHR KAQEFAIYDD EKYAHYESLG YNCKDYDHFQ
RGHCTKCSSA LQCNRWGRWF DYWPNQSRPK NWTKPIVLYI NTVGKYPFSL FHYGIKVITS
SDDFASFKGQ LSMNLTGTIR KTFHVTINLE DQFEPNSYYT HLFTLRKSLG KIVEIKAKLL
DKNLKELSTK DVWIVVERIE VTFMNGHQQS LAHKTPEKNE ATNPLDLDQS RLTSRKFFKD
HNEEIVCYSP YGCFTKNEVD NKFTIGKILA RFPEDPRKLG VQYYFFSCKD YFNPTVLPWT
LNESDLIRNL NYNPKFQTII LVHGYTERFN QLDWTGDLKD TVLNRDSCRW NVIGVEYGRA
VQSPYAQAIA NAKLVGAMIA YLIRQLNLAF NTTNNDFVLV GHSLGCHTAG FAGKKLTDPK
LRMILASEPA GPAFNRVSNS ERLSPTDADL VLTVQTNQGS SFLQGSGVKD PLGHYSFLVN
DASAQPGCQV INRMGNLFTD GLINGLYAIG GCSHARSIEL IIAYAYEDSR NDFQVMAYRC
PRYQDYDEEV CYEGYGCFNQ SEINEDHPLA SDLVASLPES PNSYVLQLFF FTCENPLNPT
IFNQNVTVDE LKRSANFNPN RRTVLIVHGR NEHYDEFLWT GDMKDLLVTR DGCEYNVISI
DYYRMTDHSY SSGVANTQVV GAVLAKLIEK LSQAFKVDAL DFICAGHSLG SHVCGFTGQR
LKSSQLGMIL GMDPAGPAFS NVHPRSRLSI DDAKLVVTIH TNAADNVIEG YGSFEPMGHY
NFFVNGGSTQ PGCDKITAKF VCSHQKSTQY AIYNETLFDN YESMGYRCPN YDDFEKGKCN
RCEEPEDCAR FGYWFTYWPH QEVGPDFTEP LIYYVDAKEK LPYSLYHYSV ILSIDAESPT
FNGRLALNLS GSIRSFYIEK HDLEAKFEAN QTYSFLMKEK KSLGRIEKIS ATISSSAGLS
FFDPHSSVDV KQIEVRYMNG FDQSTRDDLS SILTPEQSST IRSNQTTSFV YK
//