Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Active sitei77NucleophilePROSITE-ProRule annotation1
    Active sitei215Proton acceptorPROSITE-ProRule annotation1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi77S → A, D, T, N or C: Loss of esterase activity and impaired insecticidal activity. 1 Publication1
    Mutagenesisi215D → A: Loss of esterase activity and impaired insecticidal activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 23Sequence analysisAdd BLAST23
    ChainiPRO_000029671424 – 386Patatin-17Add BLAST363

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi202N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi29 – 34Combined sources6
    Helixi38 – 41Combined sources4
    Helixi42 – 58Combined sources17
    Helixi66 – 68Combined sources3
    Beta strandi71 – 75Combined sources5
    Helixi78 – 87Combined sources10
    Beta strandi93 – 97Combined sources5
    Helixi99 – 101Combined sources3
    Helixi102 – 113Combined sources12
    Beta strandi120 – 122Combined sources3
    Helixi128 – 138Combined sources11
    Helixi143 – 145Combined sources3
    Beta strandi147 – 156Combined sources10
    Turni157 – 160Combined sources4
    Beta strandi161 – 165Combined sources5
    Turni168 – 172Combined sources5
    Helixi174 – 176Combined sources3
    Helixi180 – 188Combined sources9
    Turni191 – 193Combined sources3
    Beta strandi197 – 202Combined sources6
    Beta strandi208 – 215Combined sources8
    Helixi216 – 219Combined sources4
    Helixi225 – 235Combined sources11
    Turni236 – 238Combined sources3
    Helixi240 – 245Combined sources6
    Helixi250 – 252Combined sources3
    Beta strandi253 – 258Combined sources6
    Helixi266 – 268Combined sources3
    Helixi272 – 275Combined sources4
    Helixi280 – 309Combined sources30
    Helixi313 – 315Combined sources3
    Beta strandi316 – 319Combined sources4
    Helixi326 – 329Combined sources4
    Helixi336 – 351Combined sources16
    Beta strandi352 – 355Combined sources4
    Beta strandi358 – 361Combined sources4
    Helixi362 – 381Combined sources20

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8LPW4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini32 – 229PNPLAPROSITE-ProRule annotationAdd BLAST198

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Coiled coili321 – 384Sequence analysisAdd BLAST64

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi36 – 41GXGXXGPROSITE-ProRule annotation6
    Motifi75 – 79GXSXGPROSITE-ProRule annotation5
    Motifi215 – 217DGA/GPROSITE-ProRule annotation3

    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 PNPLA (patatin-like phospholipase) domain.PROSITE-ProRule annotation

    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.
    PROSITEiPS51635. PNPLA. 1 hit.
    [Graphical view]

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1OXWX-ray2.20A/B/C23-386[»]
    4PK9X-ray1.96A23-386[»]
    4PKAX-ray2.60X23-386[»]
    4PKBX-ray2.09A23-386[»]
    ProteinModelPortaliQ8LPW4.
    SMRiQ8LPW4.
    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.
    PROSITEiPS51635. PNPLA. 1 hit.
    [Graphical view]
    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: November 30, 2016
    This is version 49 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.