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Protein

Patatin-17

Gene
N/A
Organism
Solanum cardiophyllum (Heartleaf nightshade) (Solanum cardiophyllum Lindl.)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-specific lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens (By similarity). Catalyzes the non-specific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols includng p-nitrophenyl caprate. Confers resistance to southern corn rootworm (SCRW).By similarity1 Publication

Kineticsi

  1. KM=0.26 mM for p-nitrophenyl caprate1 Publication

    pH dependencei

    Optimum pH is 5-9.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei77 – 771Nucleophile
    Active sitei215 – 2151Proton acceptor

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Storage protein

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism, Plant defense

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Patatin-17 (EC:3.1.1.-)
    OrganismiSolanum cardiophyllum (Heartleaf nightshade) (Solanum cardiophyllum Lindl.)
    Taxonomic identifieri160510 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771S → A, D, T, N or C: Loss of esterase activity and impaired insecticidal activity. 1 Publication
    Mutagenesisi215 – 2151D → A: Loss of esterase activity and impaired insecticidal activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence analysisAdd
    BLAST
    Chaini24 – 386363Patatin-17PRO_0000296714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 346Combined sources
    Helixi38 – 414Combined sources
    Helixi42 – 5817Combined sources
    Helixi66 – 683Combined sources
    Beta strandi71 – 755Combined sources
    Helixi78 – 8710Combined sources
    Beta strandi93 – 975Combined sources
    Helixi99 – 1013Combined sources
    Helixi102 – 11312Combined sources
    Beta strandi120 – 1223Combined sources
    Helixi128 – 13811Combined sources
    Helixi143 – 1453Combined sources
    Beta strandi147 – 15610Combined sources
    Turni157 – 1604Combined sources
    Beta strandi161 – 1655Combined sources
    Turni168 – 1725Combined sources
    Helixi174 – 1763Combined sources
    Helixi180 – 1889Combined sources
    Turni191 – 1933Combined sources
    Beta strandi197 – 2026Combined sources
    Beta strandi208 – 2158Combined sources
    Helixi216 – 2194Combined sources
    Helixi225 – 23511Combined sources
    Turni236 – 2383Combined sources
    Helixi240 – 2456Combined sources
    Helixi250 – 2523Combined sources
    Beta strandi253 – 2586Combined sources
    Helixi266 – 2683Combined sources
    Helixi272 – 2754Combined sources
    Helixi280 – 30930Combined sources
    Helixi313 – 3153Combined sources
    Beta strandi316 – 3194Combined sources
    Helixi326 – 3294Combined sources
    Helixi336 – 35116Combined sources
    Beta strandi352 – 3554Combined sources
    Beta strandi358 – 3614Combined sources
    Helixi362 – 38120Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OXWX-ray2.20A/B/C23-386[»]
    4PK9X-ray1.96A23-386[»]
    4PKAX-ray2.60X23-386[»]
    4PKBX-ray2.09A23-386[»]
    ProteinModelPortaliQ8LPW4.
    SMRiQ8LPW4. Positions 23-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8LPW4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 228197PatatinAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili321 – 38464Sequence analysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 404GGXR
    Motifi75 – 795GXSXG
    Motifi215 – 2173DGA

    Domaini

    The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.

    Sequence similaritiesi

    Belongs to the patatin family.Curated
    Contains 1 patatin domain.Curated

    Keywords - Domaini

    Coiled coil, Signal

    Family and domain databases

    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR002641. Patatin/PLipase_A2-rel.
    [Graphical view]
    PfamiPF01734. Patatin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52151. SSF52151. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8LPW4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATTKSFLIL IFMILATTSS TFAQLGEMVT VLSIDGGGIR GIIPATILEF
    60 70 80 90 100
    LEGQLQEMDN NADARLADYF DVIGGTSTGG LLTAMISTPN ENNRPFAAAK
    110 120 130 140 150
    EIVPFYFEHG PQIFNPSGQI LGPKYDGKYL MQVLQEKLGE TRVHQALTEV
    160 170 180 190 200
    VISSFDIKTN KPVIFTKSNL ANSPELDAKM YDISYSTAAA PTYFPPHYFV
    210 220 230 240 250
    TNTSNGDEYE FNLVDGAVAT VADPALLSIS VATRLAQKDP AFASIRSLNY
    260 270 280 290 300
    KKMLLLSLGT GTTSEFDKTY TAKEAATWTA VHWMLVIQKM TDAASSYMTD
    310 320 330 340 350
    YYLSTAFQAL DSKNNYLRVQ ENALTGTTTE MDDASEANME LLVQVGENLL
    360 370 380
    KKPVSEDNPE TYEEALKRFA KLLSDRKKLR ANKASY
    Length:386
    Mass (Da):42,486
    Last modified:October 1, 2002 - v1
    Checksum:i30C56BA86A0242E2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY033231 mRNA. Translation: AAK56395.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY033231 mRNA. Translation: AAK56395.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OXWX-ray2.20A/B/C23-386[»]
    4PK9X-ray1.96A23-386[»]
    4PKAX-ray2.60X23-386[»]
    4PKBX-ray2.09A23-386[»]
    ProteinModelPortaliQ8LPW4.
    SMRiQ8LPW4. Positions 23-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8LPW4.

    Family and domain databases

    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR002641. Patatin/PLipase_A2-rel.
    [Graphical view]
    PfamiPF01734. Patatin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52151. SSF52151. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPAT17_SOLCD
    AccessioniPrimary (citable) accession number: Q8LPW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: October 1, 2002
    Last modified: December 9, 2015
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Patatin have a dual role as a somatic storage protein and as an enzyme involved in host resistance.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.