ID A0A453BDS1_AEGTS Unreviewed; 1364 AA.
AC A0A453BDS1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20470300.4, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20470300.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
CC -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC role in disease resistance. {ECO:0000256|ARBA:ARBA00025642}.
CC -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC motif define the oxyanion hole, and stabilize the oxyanion that forms
CC during the nucleophilic attack by the catalytic serine during substrate
CC cleavage. {ECO:0000256|RuleBase:RU361262}.
CC -!- SIMILARITY: Belongs to the patatin family.
CC {ECO:0000256|RuleBase:RU361262}.
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DR STRING; 200361.A0A453BDS1; -.
DR EnsemblPlants; AET2Gv20470300.4; AET2Gv20470300.4; AET2Gv20470300.
DR Gramene; AET2Gv20470300.4; AET2Gv20470300.4; AET2Gv20470300.
DR Proteomes; UP000015105; Chromosome 2D.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045217; PNPLA8-like.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361262};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361262};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361262};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 545..819
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 21..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 150326 MW; D52C2639C2F52063 CRC64;
MSSWGLGWKR SSEIFHLTLD YGDFADEPDQ DPSSPPAPPP QSPTAASPTA SSSPVATMNG
DLGFRIELDW STSDDEDQVA LRLQSQLMVA LPPPHDVVCV DLKPADDGDD VGVEMRVVRR
REALRSVRVA RALGSTQSTG DGAVVLARLI RSNLAPAPAA DGAVAAGVPV LADHWRSVAV
LSLCNCGLMV LPVELTRLSF LEKLYIDNNK LSVLPPEVGD LKNLKVLTVD NNMLVSVPVE
LRQCVLLEEL SLEHNKLVRP LLDFRSVPKL RVLRLFGNPL EFLPEILPLH NLRHLTLANI
RIDALESLKS VTVEIETENY SYFIAARHKL SAFFSLVFRF SSCHHPLLAS ALAKIMEDRT
NQVAISKEEN AVRQLISMIS SDNRHVVEQA CLALSSLASD ISSAMQLIKC DIMKPIEAVL
KSFDDEELIS VLQVVVTLTF VSDHVAQKML RKDVLKSLKA LCAHKNSEVQ RLSLFAVGNL
AFCLETRRTL IHSESLRDLL IRSTFSQEKR VSKAAARALA ILGENENLRR AIRGRPVAKK
GLRILSMDGG GMKGLATVQM LKQIEQGTGK RIHEMFDLIC GTSTGGMLAM ALGIKQMSLD
QCEEIYTKLG ECFFGSSCFI TFLIILTLMC CQLNCCFLLF LGKLVFAEPV PKDESATWKE
KLDQLFKSSS QSFRVVVHGS KHSADQFERL LKEMCADDDG DLLIESSVKG IPKVFAVSTL
VSAMPAQPYI FRNYQYPPGT LEVSPGMAES PSTGAVGTVV SGAPVGIKRG AFMGSCKHHV
WEAIRASSAA PYYLDDFSDD VNRWQDGAIV ANNPTIFAIR EAQLLWPDTR IDCLVSIGCG
SVPTKSRRGG WRYLDTGQVL IESACSVERV EETLDTLIPM LPEMQYFRFN PVDDRCGMEL
DETDPAVWLK LEAATEEYIQ KNLDVFKNVC ELLVPRYQEE EKSSGIVKSL SFSRLSTSKS
GLSESNPTLG WRRVVLLVEA SFNPDFGKKI NHTRSLEAFC SQNGIRLTLM NSTSGFGKPT
TALPTPITSP LFTGSFPSSP LLYSPEGTQR IGRIDLVPPL SLDGHPAMKS SPPTSPIKSW
QPSGHVRSLY DKLQNMPQVG VIHLALQNDS TGSILSWQND VFVVAEPGEL ADRFLQCVKT
SLSTMLHGSK RTGAYSVSKI SCLSELVAEW PSFEIGGIHH RYIGRQTQVM EDNQEIGAYM
FRRTVPACHM SPEDVRWMVG AWRERIIVCS GKYGFVHGLI KAFVDSGAKA IISSSVEPPD
SQAIAYHGMD VSGSLENGKF VIGDDEADES EPEPVSPISD WEDSDAEKNG EGNKDIDEEE
YLAQFICLLY DKLFREGVTV DTALQQALRA HPRLKYSCHL PNVS
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