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Antimicrobial peptides (IB-AMP) [Cleaved into: Basic peptide AMP3 (IB-AMP3); Basic peptide AMP1-1 (IB-AMP1-1); Basic peptide AMP1-2 (IB-AMP1-2); Basic peptide AMP1-3 (IB-AMP1-3); Basic peptide AMP2 (IB-AMP2); Basic peptide AMP4 (IB-AMP4)]

 AMP_IMPBA               Reviewed;         333 AA.
O24006;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 58.
RecName: Full=Antimicrobial peptides;
AltName: Full=IB-AMP;
Contains:
RecName: Full=Basic peptide AMP3;
AltName: Full=IB-AMP3;
Contains:
RecName: Full=Basic peptide AMP1-1;
AltName: Full=IB-AMP1-1;
Contains:
RecName: Full=Basic peptide AMP1-2;
AltName: Full=IB-AMP1-2;
Contains:
RecName: Full=Basic peptide AMP1-3;
AltName: Full=IB-AMP1-3;
Contains:
RecName: Full=Basic peptide AMP2;
AltName: Full=IB-AMP2;
Contains:
RecName: Full=Basic peptide AMP4;
AltName: Full=IB-AMP4;
Flags: Precursor;
Name=AMP;
Impatiens balsamina (Balsam).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; Ericales; Balsaminaceae; Impatiens; Impatiens;
Impatiens sect. Uniflorae.
NCBI_TaxID=63779;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
FORMATION AT GLN-55; GLN-103; GLN-149; GLN-197; GLN-233 AND GLN-279,
AND MASS SPECTROMETRY.
TISSUE=Seed;
PubMed=9305910; DOI=10.1074/jbc.272.39.24480;
Tailor R.H., Acland D.P., Attenborough S., Cammue B.P.A., Evans I.J.,
Osborn R.W., Ray J.A., Rees S.B., Broekaert W.F.;
"A novel family of small cysteine-rich antimicrobial peptides from
seed of Impatiens balsamina is derived from a single precursor
protein.";
J. Biol. Chem. 272:24480-24487(1997).
[2]
STRUCTURE BY NMR OF IB-AMP1.
PubMed=9454588; DOI=10.1021/bi971747d;
Patel S.U., Osborn R.W., Rees S.B., Thornton J.M.;
"Structural studies of Impatiens balsamina antimicrobial protein (Ib-
AMP1).";
Biochemistry 37:983-990(1998).
-!- FUNCTION: Plays a role in the defense of the germinating seed
against micro-organisms, by inhibiting the growth of a range of
filamentous fungi and bacteria, especially Gram-positive bacteria.
Not cytotoxic for cultured human cells and are the smallest known
plant-derived antimicrobial peptides. Peptide IB-AMP4 has a higher
antifungal activity than IB-AMP1.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DEVELOPMENTAL STAGE: Highly expressed in dry mature seed and by
the stages 2-5 of developing seed. The peptide IB-AMP1 is also
detected at early stages of germination (24 hours and 48 hours
postgermination).
-!- DOMAIN: Contains repeated alternating basic mature peptide and
acidic propeptide domains.
-!- PTM: The N-terminal of all peptides are blocked.
-!- PTM: The 4 cysteine residues of all peptides are involved in
intrachain disulfide bonds.
-!- MASS SPECTROMETRY: Mass=2536.6; Method=Electrospray; Range=55-74;
Evidence={ECO:0000269|PubMed:9305910};
-!- MASS SPECTROMETRY: Mass=2464.6; Method=Electrospray; Range=103-
122; Evidence={ECO:0000269|PubMed:9305910};
-!- MASS SPECTROMETRY: Mass=2527.4; Method=Electrospray; Range=233-
252; Evidence={ECO:0000269|PubMed:9305910};
-!- MASS SPECTROMETRY: Mass=2522.6; Method=Electrospray; Range=279-
298; Evidence={ECO:0000269|PubMed:9305910};
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EMBL; Y14369; CAA74738.1; -; mRNA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
Direct protein sequencing; Disulfide bond; Fungicide; Plant defense;
Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 54 Acidic peptide 1.
/FTId=PRO_0000020710.
PEPTIDE 55 74 Basic peptide AMP3.
/FTId=PRO_0000020711.
PROPEP 75 102 Acidic peptide 2.
/FTId=PRO_0000020712.
PEPTIDE 103 122 Basic peptide AMP1-1.
/FTId=PRO_0000020713.
PROPEP 123 148 Acidic peptide 3.
/FTId=PRO_0000020714.
PEPTIDE 149 168 Basic peptide AMP1-2.
/FTId=PRO_0000020715.
PROPEP 169 196 Acidic peptide 4.
/FTId=PRO_0000020716.
PEPTIDE 197 216 Basic peptide AMP1-3.
/FTId=PRO_0000020717.
PROPEP 217 232 Acidic peptide 5.
/FTId=PRO_0000020718.
PEPTIDE 233 252 Basic peptide AMP2.
/FTId=PRO_0000020719.
PROPEP 253 278 Acidic peptide 6.
/FTId=PRO_0000020720.
PEPTIDE 279 298 Basic peptide AMP4.
/FTId=PRO_0000020721.
PROPEP 299 333 Acidic peptide 7.
/FTId=PRO_0000020722.
MOD_RES 55 55 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
MOD_RES 103 103 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
MOD_RES 149 149 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
MOD_RES 197 197 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
MOD_RES 233 233 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
MOD_RES 279 279 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9305910}.
DISULFID 60 70 {ECO:0000250}.
DISULFID 61 74 {ECO:0000250}.
DISULFID 108 118
DISULFID 109 122
DISULFID 154 164
DISULFID 155 168
DISULFID 202 212
DISULFID 203 216
DISULFID 238 248 {ECO:0000250}.
DISULFID 239 252 {ECO:0000250}.
DISULFID 284 294 {ECO:0000250}.
DISULFID 285 298 {ECO:0000250}.
SEQUENCE 333 AA; 37259 MW; A3B2BE2D9184407D CRC64;
MVQKGVVFGV LLILFICSTL TSADSKPNPT KEEEPAKKPD EVSVKSGGPE VSEDQYRHRC
CAWGPGRKYC KRWCANAEEA AAAIPEASEE LAQEEAPVYS EDQWGRRCCG WGPGRRYCVR
WCQNAEEAAA AIPEATEKAQ EAPVYSEDQW GRRCCGWGPG RRYCVRWCQN AEEAAAAVAI
PEASEKAQEG PVYSEDQWGR RCCGWGPGRR YCVRWCSNAA DEVATPEDVE PGQYGRRCCN
WGPGRRYCKR WCHNAAEEAT LKAFEEEAAR EQPVYSEDQW GRRCCGWGPG RRYCRRWCQS
AEEAAAFQAG EVTASLMLIM FKACPCMGPV PSV


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