SNAK1_SOLTU
ID SNAK1_SOLTU Reviewed; 88 AA.
AC Q948Z4; Q9ZTX6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Snakin-1;
DE Flags: Precursor;
GN Name=SN1;
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], PROTEIN SEQUENCE OF 26-60, FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Jaerla; TISSUE=Tuber;
RX PubMed=9885189; DOI=10.1094/mpmi.1999.12.1.16;
RA Segura A., Moreno M., Madueno F., Molina A., Garcia-Olmedo F.;
RT "Snakin-1, a peptide from potato that is active against plant pathogens.";
RL Mol. Plant Microbe Interact. 12:16-23(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Berrocal Lobo M.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has an antimicrobial activity. Causes a rapid aggregation of
CC both Gram-positive and Gram-negative bacteria, but the antimicrobial
CC activity is not correlated with the capacity to aggregate bacteria.
CC {ECO:0000269|PubMed:9885189}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC -!- TISSUE SPECIFICITY: Expressed in tubers, stems, axillary and young
CC floral buds, sepals, petals, stamens and carpels, but not in roots,
CC stolons, shoot apex meristem or young leaves.
CC {ECO:0000269|PubMed:9885189}.
CC -!- INDUCTION: No responses to methyl jasmonate, ethylene, abscisic acid,
CC salicylic acid, isonicotinic acid, indolacetic acid, gibberellic acid
CC and infection with incompatible bacterial or compatible fungual
CC pathogens. {ECO:0000269|PubMed:9885189}.
CC -!- PTM: Six disulfide bonds may be present.
CC -!- SIMILARITY: Belongs to the GASA family. {ECO:0000305}.
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DR EMBL; AF014396; AAD01518.1; -; mRNA.
DR EMBL; AJ320185; CAC44032.1; -; Genomic_DNA.
DR PDB; 5E5Q; X-ray; 1.60 A; A/B=29-88.
DR PDB; 5E5T; X-ray; 1.57 A; A/C=29-88, B/D=26-83.
DR PDB; 5E5Y; X-ray; 1.51 A; A/C=29-88, B/D=26-83.
DR PDBsum; 5E5Q; -.
DR PDBsum; 5E5T; -.
DR PDBsum; 5E5Y; -.
DR AlphaFoldDB; Q948Z4; -.
DR SMR; Q948Z4; -.
DR STRING; 4113.PGSC0003DMT400055426; -.
DR eggNOG; ENOG502S46W; Eukaryota.
DR InParanoid; Q948Z4; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q948Z4; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR003854; GASA.
DR Pfam; PF02704; GASA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Cell wall; Direct protein sequencing;
KW Disulfide bond; Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..88
FT /note="Snakin-1"
FT /id="PRO_0000348599"
FT CONFLICT 28
FT /note="S -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5E5Y"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5E5Y"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:5E5Y"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:5E5Y"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5E5Y"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:5E5Y"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5E5Y"
SQ SEQUENCE 88 AA; 9664 MW; 0F31E83EF61E7D09 CRC64;
MKLFLLTLLL VTLVITPSLI QTTMAGSSFC DSKCKLRCSK AGLADRCLKY CGICCEECKC
VPSGTYGNKH ECPCYRDKKN SKGKSKCP
