DEF_NICSU
ID DEF_NICSU Reviewed; 47 AA.
AC C0HK49;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Defensin NsD7 {ECO:0000303|PubMed:27647905};
OS Nicotiana suaveolens (Australian tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=200320;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-47 IN COMPLEX
RP WITH PHOSPHATIDIC ACID, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS
RP OF LYS-4; ILE-15; ARG-26; LYS-36; ILE-37 AND ARG-39.
RX PubMed=27647905; DOI=10.1073/pnas.1607855113;
RA Kvansakul M., Lay F.T., Adda C.G., Veneer P.K., Baxter A.A., Phan T.K.,
RA Poon I.K., Hulett M.D.;
RT "Binding of phosphatidic acid by NsD7 mediates the formation of helical
RT defensin-lipid oligomeric assemblies and membrane permeabilization.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:11202-11207(2016).
CC -!- FUNCTION: Plant defense peptide (Probable). Disrupts membranes
CC containing phosphatidic acid (PA) via a PA-dependent oligomerization
CC process. {ECO:0000269|PubMed:27647905, ECO:0000303|PubMed:27647905}.
CC -!- SUBUNIT: In the presence of phosphatidic acid (PA), forms right-handed
CC double helices which tend to bundle into fibrils. Each helix is a
CC repetition of dimers containing 2 bound molecules of PA per dimer.
CC Dimers are arranged orthogonally in a tip-to-tip configuration with 1
CC molecule of PA located at the dimer contact interface. Association of 2
CC helices to form a double helix depends on intercalating isoleucine
CC residues Ile-15 and Ile-37. Bundling of double helices into fibrils
CC depends on Arg-26. {ECO:0000269|PubMed:27647905}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:Q8GTM0}.
CC -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR PDB; 5KK4; X-ray; 1.70 A; A/B/C/D/E/F=1-47.
DR PDB; 5VYP; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-47.
DR PDBsum; 5KK4; -.
DR PDBsum; 5VYP; -.
DR AlphaFoldDB; C0HK49; -.
DR SMR; C0HK49; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR CDD; cd00107; Knot1; 1.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR008176; Defensin_plant.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR PRINTS; PR00288; PUROTHIONIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Lipid-binding; Plant defense; Vacuole.
FT CHAIN 1..47
FT /note="Defensin NsD7"
FT /id="PRO_0000438709"
FT BINDING 4
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27647905"
FT BINDING 33
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27647905"
FT BINDING 36
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two adjacent subunits"
FT /evidence="ECO:0000269|PubMed:27647905"
FT BINDING 39
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two adjacent subunits"
FT /evidence="ECO:0000269|PubMed:27647905"
FT SITE 15
FT /note="Required for formation of double helix"
FT /evidence="ECO:0000269|PubMed:27647905"
FT SITE 37
FT /note="Required for formation of double helix"
FT /evidence="ECO:0000269|PubMed:27647905"
FT DISULFID 3..47
FT /evidence="ECO:0000269|PubMed:27647905"
FT DISULFID 14..34
FT /evidence="ECO:0000269|PubMed:27647905"
FT DISULFID 20..41
FT /evidence="ECO:0000269|PubMed:27647905"
FT DISULFID 24..43
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 4
FT /note="K->E: Unperturbed ability for fibril formation and
FT membrane disrupting activity."
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 15
FT /note="I->D: Complete loss of fibril formation and of
FT membrane disrupting activity."
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 26
FT /note="R->A: Retains double helix formation and membrane
FT disrupting activity, although no fibrils are formed."
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 36
FT /note="K->E: Complete loss of fibril formation, although
FT some higher-order oligomers are still formed, and of
FT membrane disrupting activity."
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 37
FT /note="I->D: Loss of fibril formation, although some
FT higher-order oligomers are still formed, and of membrane
FT disrupting activity."
FT /evidence="ECO:0000269|PubMed:27647905"
FT MUTAGEN 39
FT /note="R->E: Complete loss of oligomerization, fibril
FT formation and of membrane disrupting activity."
FT /evidence="ECO:0000269|PubMed:27647905"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5KK4"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:5KK4"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5KK4"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5KK4"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5KK4"
SQ SEQUENCE 47 AA; 5386 MW; 2DFCE619D2A1BD2A CRC64;
KDCKRESNTF PGICITKPPC RKACIREKFT DGHCSKILRR CLCTKPC
