ID A0A182RCA6_ANOFN Unreviewed; 398 AA.
AC A0A182RCA6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN003822-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN003822-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN003822-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR AlphaFoldDB; A0A182RCA6; -.
DR STRING; 62324.A0A182RCA6; -.
DR EnsemblMetazoa; AFUN003822-RA; AFUN003822-PA; AFUN003822.
DR VEuPathDB; VectorBase:AFUN003822; -.
DR VEuPathDB; VectorBase:AFUN2_007848; -.
DR OrthoDB; 3413176at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF100; LIPASE-RELATED; 1.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR000862};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..398
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030024173"
FT DOMAIN 67..369
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 398 AA; 44618 MW; C7CA787742A9911F CRC64;
MAGIVALRLI LTLVIFTVHV LCAKKPAEIL RHSVTRHGYP VELHKVTTQD GYILSLVRIP
GKSDKAPVLI VHGLLSSSVD WTVQGPDKSI SFIAADEGYD VWLGNVRGNT FSKEHKTFSS
KDREYWQFSF HEIGMYDIPA MVDYIRSNTS SDTVHYIGHS QGGTVFLVMA SMRPAYNIKF
ASVHLMAPAA YIYHATSPAV DFASRIDELE MFAKLTRSYE IGGRGPGSSI DLVYAGHKTG
LVPTSLVLTN IWYLVGVHDS INRTVLGEIL ANTPAGCSVY QLLHFGQNYL AKAFQLYDYG
RVANMQRYGA KIPPEYPLHN VTAPIMLYYS AGDNFVPPED VEELADQLPN VVHKHRIGLR
KWNHIDYMFD TSAHRLYRMI VASLRNQSTD ENRSQVTH
//