PAT17_SOLCD
ID PAT17_SOLCD Reviewed; 386 AA.
AC Q8LPW4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Patatin-17;
DE EC=3.1.1.-;
DE Flags: Precursor;
OS Solanum cardiophyllum (Heartleaf nightshade) (Solanum cardiophyllum
OS Lindl.).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=160510;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF
RP 23-386, MUTAGENESIS OF SER-77 AND ASP-215, FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12779324; DOI=10.1021/bi027156r;
RA Rydel T.J., Williams J.M., Krieger E., Moshiri F., Stallings W.C.,
RA Brown S.M., Pershing J.C., Purcell J.P., Alibhai M.F.;
RT "The crystal structure, mutagenesis, and activity studies reveal that
RT patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad.";
RL Biochemistry 42:6696-6708(2003).
CC -!- FUNCTION: Non-specific lipolytic acyl hydrolase (LAH), an activity
CC which is thought to be involved in the response of tubers to pathogens
CC (By similarity). Catalyzes the non-specific hydrolysis of
CC phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols
CC includng p-nitrophenyl caprate. Confers resistance to southern corn
CC rootworm (SCRW). {ECO:0000250, ECO:0000269|PubMed:12779324}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for p-nitrophenyl caprate {ECO:0000269|PubMed:12779324};
CC pH dependence:
CC Optimum pH is 5-9.5. {ECO:0000269|PubMed:12779324};
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.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; AY033231; AAK56395.1; -; mRNA.
DR PDB; 1OXW; X-ray; 2.20 A; A/B/C=23-386.
DR PDB; 4PK9; X-ray; 1.96 A; A=23-386.
DR PDB; 4PKA; X-ray; 2.60 A; X=23-386.
DR PDB; 4PKB; X-ray; 2.09 A; A=23-386.
DR PDBsum; 1OXW; -.
DR PDBsum; 4PK9; -.
DR PDBsum; 4PKA; -.
DR PDBsum; 4PKB; -.
DR AlphaFoldDB; Q8LPW4; -.
DR SMR; Q8LPW4; -.
DR PRIDE; Q8LPW4; -.
DR EvolutionaryTrace; Q8LPW4; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IEA:UniProt.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
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 3D-structure; Coiled coil; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Plant defense; Signal; Storage protein; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..386
FT /note="Patatin-17"
FT /id="PRO_0000296714"
FT DOMAIN 32..229
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COILED 321..384
FT /evidence="ECO:0000255"
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 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 77
FT /note="S->A,D,T,N,C: Loss of esterase activity and impaired
FT insecticidal activity."
FT /evidence="ECO:0000269|PubMed:12779324"
FT MUTAGEN 215
FT /note="D->A: Loss of esterase activity and impaired
FT insecticidal activity."
FT /evidence="ECO:0000269|PubMed:12779324"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:4PK9"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4PK9"
FT TURN 168..172
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:4PK9"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4PK9"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 280..309
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 336..351
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:4PK9"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4PK9"
FT HELIX 362..381
FT /evidence="ECO:0007829|PDB:4PK9"
SQ SEQUENCE 386 AA; 42486 MW; 30C56BA86A0242E2 CRC64;
MATTKSFLIL IFMILATTSS TFAQLGEMVT VLSIDGGGIR GIIPATILEF LEGQLQEMDN
NADARLADYF DVIGGTSTGG LLTAMISTPN ENNRPFAAAK EIVPFYFEHG PQIFNPSGQI
LGPKYDGKYL MQVLQEKLGE TRVHQALTEV VISSFDIKTN KPVIFTKSNL ANSPELDAKM
YDISYSTAAA PTYFPPHYFV TNTSNGDEYE FNLVDGAVAT VADPALLSIS VATRLAQKDP
AFASIRSLNY KKMLLLSLGT GTTSEFDKTY TAKEAATWTA VHWMLVIQKM TDAASSYMTD
YYLSTAFQAL DSKNNYLRVQ ENALTGTTTE MDDASEANME LLVQVGENLL KKPVSEDNPE
TYEEALKRFA KLLSDRKKLR ANKASY
