PATB2_SOLTU
ID PATB2_SOLTU Reviewed; 386 AA.
AC P15477;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Patatin-B2;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=PATB2;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bintje;
RX AGRICOLA=IND92000050; DOI=10.1007/BF00027383;
RA Stiekema W.J., Heidekamp F., Dirkse W.G., van Beckum J., de Haan P.,
RA ten Bosch C., Louwerse J.D.;
RT "Molecular cloning and analysis of four potato tuber mRNAs.";
RL Plant Mol. Biol. 11:255-269(1988).
RN [2]
RP FUNCTION, MUTAGENESIS OF SER-33; LYS-40; SER-77; HIS-198; ASP-215 AND
RP SER-257, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION BY
RP METHYL-P-NITROPHENYL-OCTYLPHOSPHONATE.
RX PubMed=11589694; DOI=10.1046/j.0014-2956.2001.02411.x;
RA Hirschberg H.J.H.B., Simons J.-W.F.A., Dekker N., Egmond M.R.;
RT "Cloning, expression, purification and characterization of patatin, a novel
RT phospholipase A.";
RL Eur. J. Biochem. 268:5037-5044(2001).
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH), an activity which is thought
CC to be involved in the response of tubers to pathogens. Can use p-
CC nitrophenyl esters as substrates with highest activity on p-nitrophenyl
CC caprate (C10). Also active on mono-acylglycolphosphocholines and
CC diacylphospholipids, with highest specific activities observed were
CC obtained with the synthetic phospholipids diC8PCho and diC9PCho. Mono-
CC olein and myverol can also be hydrolyzed.
CC {ECO:0000269|PubMed:11589694}.
CC -!- ACTIVITY REGULATION: Inhibited by methyl-p-nitrophenyl-
CC octylphosphonate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=At pH 8.0, the highest specific activity is observed with
CC phospholipids such as diC8PCho and diC9PCho and with p-nitrophenyl
CC esters such as p-nitrophenyl caprate. {ECO:0000269|PubMed:11589694};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
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.
CC -!- MISCELLANEOUS: Patatin have a dual role as a somatic storage protein
CC and as an enzyme involved in host resistance. This tuber protein
CC represents approximately 40% of the total protein in mature tubers.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X13178; CAA31575.1; -; mRNA.
DR PIR; S05592; S05592.
DR AlphaFoldDB; P15477; -.
DR SMR; P15477; -.
DR Allergome; 639; Sola t 1.
DR PRIDE; P15477; -.
DR InParanoid; P15477; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P15477; baseline and differential.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Plant defense; Reference proteome; Signal; Storage protein; Vacuole.
FT SIGNAL 1..23
FT CHAIN 24..386
FT /note="Patatin-B2"
FT /id="PRO_0000032258"
FT DOMAIN 32..229
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 36..41
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 75..79
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 215..217
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 33
FT /note="S->C,T: Reduced hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
FT MUTAGEN 40
FT /note="K->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
FT MUTAGEN 77
FT /note="S->A,C,T: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
FT MUTAGEN 198
FT /note="H->N: Reduced hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
FT MUTAGEN 215
FT /note="D->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
FT MUTAGEN 257
FT /note="S->C,T: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11589694"
SQ SEQUENCE 386 AA; 42613 MW; 5C0518B68A282405 CRC64;
MATTKSFLIL FFMILATTSS TCAKLEEMVT VLSIDGGGIK GIIPAIILEF LEGQLQEVDN
NKDARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIVPFYFEHG PHIFNYSGSI
LGPMYDGKYL LQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
YDICYSTAAA PIYFPPHHFV THTSNGARYE FNLVDGAVAT VGDPALLSLS VATRLAQEDP
AFSSIKSLDY KQMLLLSLGT GTNSEFDKTY TAEEAAKWGP LRWMLAIQQM TNAASSYMTD
YYISTVFQAR HSQNNYLRVQ ENALNGTTTE MDDASEANME LLVQVGETLL KKPVSKDSPE
TYEEALKRFA KLLSDRKKLR ANKASH
