AMP_IMPBA
ID AMP_IMPBA Reviewed; 333 AA.
AC O24006;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Antimicrobial peptides;
DE AltName: Full=IB-AMP;
DE Contains:
DE RecName: Full=Basic peptide AMP3;
DE AltName: Full=IB-AMP3;
DE Contains:
DE RecName: Full=Basic peptide AMP1-1;
DE AltName: Full=IB-AMP1-1;
DE Contains:
DE RecName: Full=Basic peptide AMP1-2;
DE AltName: Full=IB-AMP1-2;
DE Contains:
DE RecName: Full=Basic peptide AMP1-3;
DE AltName: Full=IB-AMP1-3;
DE Contains:
DE RecName: Full=Basic peptide AMP2;
DE AltName: Full=IB-AMP2;
DE Contains:
DE RecName: Full=Basic peptide AMP4;
DE AltName: Full=IB-AMP4;
DE Flags: Precursor;
GN Name=AMP;
OS Impatiens balsamina (Balsam).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Balsaminaceae; Impatiens; Impatiens subgen. Impatiens;
OC Impatiens sect. Uniflorae.
OX NCBI_TaxID=63779;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
RP FORMATION AT GLN-55; GLN-103; GLN-149; GLN-197; GLN-233 AND GLN-279, AND
RP MASS SPECTROMETRY.
RC TISSUE=Seed;
RX PubMed=9305910; DOI=10.1074/jbc.272.39.24480;
RA Tailor R.H., Acland D.P., Attenborough S., Cammue B.P.A., Evans I.J.,
RA Osborn R.W., Ray J.A., Rees S.B., Broekaert W.F.;
RT "A novel family of small cysteine-rich antimicrobial peptides from seed of
RT Impatiens balsamina is derived from a single precursor protein.";
RL J. Biol. Chem. 272:24480-24487(1997).
RN [2]
RP STRUCTURE BY NMR OF IB-AMP1.
RX PubMed=9454588; DOI=10.1021/bi971747d;
RA Patel S.U., Osborn R.W., Rees S.B., Thornton J.M.;
RT "Structural studies of Impatiens balsamina antimicrobial protein (Ib-
RT AMP1).";
RL Biochemistry 37:983-990(1998).
CC -!- FUNCTION: Plays a role in the defense of the germinating seed against
CC microorganisms, by inhibiting the growth of a range of filamentous
CC fungi and bacteria, especially Gram-positive bacteria. Not cytotoxic
CC for cultured human cells and are the smallest known plant-derived
CC antimicrobial peptides. Peptide IB-AMP4 has a higher antifungal
CC activity than IB-AMP1.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in dry mature seed and by the
CC stages 2-5 of developing seed. The peptide IB-AMP1 is also detected at
CC early stages of germination (24 hours and 48 hours postgermination).
CC -!- DOMAIN: Contains repeated alternating basic mature peptide and acidic
CC propeptide domains.
CC -!- PTM: The N-terminal of all peptides are blocked.
CC -!- PTM: The 4 cysteine residues of all peptides are involved in intrachain
CC disulfide bonds.
CC -!- MASS SPECTROMETRY: [Basic peptide AMP3]: Mass=2536.6;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:9305910};
CC -!- MASS SPECTROMETRY: [Basic peptide AMP1-1]: Mass=2464.6;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:9305910};
CC -!- MASS SPECTROMETRY: [Basic peptide AMP2]: Mass=2527.4;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:9305910};
CC -!- MASS SPECTROMETRY: [Basic peptide AMP4]: Mass=2522.6;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:9305910};
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DR EMBL; Y14369; CAA74738.1; -; mRNA.
DR AlphaFoldDB; O24006; -.
DR PRIDE; O24006; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Fungicide; Plant defense;
KW Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..54
FT /note="Acidic peptide 1"
FT /id="PRO_0000020710"
FT PEPTIDE 55..74
FT /note="Basic peptide AMP3"
FT /id="PRO_0000020711"
FT PROPEP 75..102
FT /note="Acidic peptide 2"
FT /id="PRO_0000020712"
FT PEPTIDE 103..122
FT /note="Basic peptide AMP1-1"
FT /id="PRO_0000020713"
FT PROPEP 123..148
FT /note="Acidic peptide 3"
FT /id="PRO_0000020714"
FT PEPTIDE 149..168
FT /note="Basic peptide AMP1-2"
FT /id="PRO_0000020715"
FT PROPEP 169..196
FT /note="Acidic peptide 4"
FT /id="PRO_0000020716"
FT PEPTIDE 197..216
FT /note="Basic peptide AMP1-3"
FT /id="PRO_0000020717"
FT PROPEP 217..232
FT /note="Acidic peptide 5"
FT /id="PRO_0000020718"
FT PEPTIDE 233..252
FT /note="Basic peptide AMP2"
FT /id="PRO_0000020719"
FT PROPEP 253..278
FT /note="Acidic peptide 6"
FT /id="PRO_0000020720"
FT PEPTIDE 279..298
FT /note="Basic peptide AMP4"
FT /id="PRO_0000020721"
FT PROPEP 299..333
FT /note="Acidic peptide 7"
FT /id="PRO_0000020722"
FT REGION 23..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT MOD_RES 103
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT MOD_RES 149
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT MOD_RES 197
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT MOD_RES 233
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT MOD_RES 279
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9305910"
FT DISULFID 60..70
FT /evidence="ECO:0000250"
FT DISULFID 61..74
FT /evidence="ECO:0000250"
FT DISULFID 108..118
FT DISULFID 109..122
FT DISULFID 154..164
FT DISULFID 155..168
FT DISULFID 202..212
FT DISULFID 203..216
FT DISULFID 238..248
FT /evidence="ECO:0000250"
FT DISULFID 239..252
FT /evidence="ECO:0000250"
FT DISULFID 284..294
FT /evidence="ECO:0000250"
FT DISULFID 285..298
FT /evidence="ECO:0000250"
SQ 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
