ID A0A0L9U6X8_PHAAN Unreviewed; 415 AA.
AC A0A0L9U6X8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN ORFNames=LR48_Vigan03g181400 {ECO:0000313|EMBL:KOM38432.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM38432.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR EMBL; CM003373; KOM38432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9U6X8; -.
DR STRING; 3914.A0A0L9U6X8; -.
DR EnsemblPlants; KOM38432; KOM38432; LR48_Vigan03g181400.
DR Gramene; KOM38432; KOM38432; LR48_Vigan03g181400.
DR OMA; MFGTKGF; -.
DR Proteomes; UP000053144; Chromosome 3.
DR GO; GO:0016298; F:lipase activity; IEA:EnsemblPlants.
DR GO; GO:0002213; P:defense response to insect; IEA:EnsemblPlants.
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; IPR006693; AB_hydrolase_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF99; TRIACYLGLYCEROL LIPASE 2; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000862};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..415
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005595334"
FT DOMAIN 50..108
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 388
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 415 AA; 45909 MW; 249124F2CB3D9FE5 CRC64;
MALQGSMTFA AFTFFLLLTT LPHEPHASSR GSFGRNINPP VSGLCSSSVI VHGYECQEHE
VTTNDGYILS VQRIPQGRGG KGSGSRTSKQ PVIIQHGVLV DGVTWLLNSP EQDLPLILAD
NGFDVWIANS RGTRFSRRHI SLDPSSPAFW NWSWDELVSY DLPAVFNYVF SQTEQKINYV
GHSLGTLIAL ASFSEGTLVN QLNSAALLSP IAYLSHMNTA LGVIAAKSFV GEVTTLFGLA
EFNPKGLPVD AFLKSLCVYP GIDCYDLMTA LTGLSKNCCL NSSTVDLFLM NEPQSTSTKN
MVHLAQTVRR GVLTKFNYVR PDYNIMHYGE IFPPIYNLSN IPHDLPLFIS YGGRDALSDA
RDVENLLDKL KFHDEDKLSV QFIEEYAHAD YVMGFNAKDL VYNAVVSFFN HQVNT
//
