AMP1_STEME
ID AMP1_STEME Reviewed; 167 AA.
AC E1UYT9;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Antimicrobial peptide 1 {ECO:0000303|PubMed:21706181};
DE Short=SmAMP1 {ECO:0000303|PubMed:21706181};
DE Contains:
DE RecName: Full=Antimicrobial peptide 1.1a {ECO:0000305|PubMed:21706181};
DE Short=SmAMP1.1a {ECO:0000303|PubMed:28038935};
DE Short=SmMP1.1a {ECO:0000303|PubMed:21706181};
DE Contains:
DE RecName: Full=Antimicrobial peptide 1.2a {ECO:0000305|Ref.3};
DE Short=Sm-AMP-1.2a {ECO:0000303|Ref.3};
DE Flags: Precursor;
OS Stellaria media (Common chickweed) (Alsine media).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Alsineae; Stellaria.
OX NCBI_TaxID=13274 {ECO:0000312|EMBL:CBJ21248.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Seed {ECO:0000303|PubMed:21706181};
RX PubMed=21706181; DOI=10.1007/s11248-011-9534-6;
RA Shukurov R., Voblikova V., Nikonorova A.K., Komakhin R.A., Komakhina V.,
RA Egorov T., Grishin E., Babakov A.;
RT "Transformation of tobacco and Arabidopsis plants with Stellaria media
RT genes encoding novel hevein-like peptides increases their resistance to
RT fungal pathogens.";
RL Transgenic Res. 21:313-325(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 23-57, AND FUNCTION.
RC TISSUE=Seed {ECO:0000303|PubMed:28038935};
RX PubMed=28038935; DOI=10.1016/j.biochi.2016.12.017;
RA Slavokhotova A.A., Shelenkov A.A., Korostyleva T.V., Rogozhin E.A.,
RA Melnikova N.V., Kudryavtseva A.V., Odintsova T.I.;
RT "Defense peptide repertoire of Stellaria media predicted by high throughput
RT next generation sequencing.";
RL Biochimie 135:15-27(2017).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 23-57 AND 68-100, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|Ref.3};
RA Vassilevski A.A., Musolyamov A.K., Babakov A.V., Grishin E.V., Egorov T.A.;
RL Submitted (JAN-2010) to UniProtKB.
RN [4] {ECO:0000305}
RP STRUCTURE BY NMR OF 23-57, AND DISULFIDE BONDS.
RA Bozin T.N., Bocharov E.V., Sobol V.A., Vassilevski A.A., Arseniev A.A.;
RT "Spatial structure of Antimicrobial Peptide Sm-AMP-1.1a.";
RL Submitted (FEB-2010) to the PDB data bank.
CC -!- FUNCTION: [Antimicrobial peptide 1.1a]: Antimicrobial peptide active
CC against the fungus A.alternata (IC(50)=8.6 uM) and the oomycetes
CC P.infestans OSV 12 (IC(50)=11 uM) and P.infestans PRILL 2 (IC(50)=6.5
CC uM). {ECO:0000269|PubMed:28038935}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and, to a lesser
CC extent, in stem and leaves. {ECO:0000269|PubMed:21706181}.
CC -!- INDUCTION: Strongly induced (up to 70-fold) by infection with
CC phytopathogenic fungi like R.solanum, F.culmorum and B.cinerea.
CC {ECO:0000269|PubMed:21706181}.
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1.1a]: Mass=3463.1;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 1.1a.;
CC Evidence={ECO:0000269|Ref.3};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1.2a]: Mass=3163.7;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 1.2a.;
CC Evidence={ECO:0000269|Ref.3};
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DR EMBL; FN663151; CBJ21248.1; -; mRNA.
DR PDB; 2KUS; NMR; -; A=23-57.
DR PDBsum; 2KUS; -.
DR AlphaFoldDB; E1UYT9; -.
DR SMR; E1UYT9; -.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR Gene3D; 3.30.60.10; -; 2.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SUPFAM; SSF57016; SSF57016; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 2.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Fungicide; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..57
FT /note="Antimicrobial peptide 1.1a"
FT /evidence="ECO:0000269|PubMed:28038935, ECO:0000269|Ref.3"
FT /id="PRO_0000443551"
FT PROPEP 58..67
FT /evidence="ECO:0000305|Ref.3"
FT /id="PRO_0000443552"
FT PEPTIDE 68..100
FT /note="Antimicrobial peptide 1.2a"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000443553"
FT PROPEP 101..167
FT /evidence="ECO:0000305|Ref.3"
FT /id="PRO_0000443554"
FT DOMAIN 26..66
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 69..108
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 29..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:2KUS"
FT DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:2KUS"
FT DISULFID 41..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:2KUS"
FT DISULFID 72..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 78..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 83..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 102..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 167 AA; 17251 MW; E69B0E5BD35BF941 CRC64;
MLNMKSFALV MLFATLVGVT IASGPNGQCG PGWGGCRGGL CCSQYGYCGS GPKYCAHNTP
LSEIEPTDAG RCSGRGTCSG GRCCSKYGYC GTGPAYCGLG MCQGSCLPDM PNHPAQIQAR
TEAAQAEAQA EAYNQANEAA QVEAYYQATQ AQTQAQPQVE PAVTKAP
