AMP_TRIKH
ID AMP_TRIKH Reviewed; 116 AA.
AC P85966; H6S4F1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Antimicrobial peptide 1b {ECO:0000303|PubMed:19583772};
DE Short=WAMP-1b {ECO:0000303|PubMed:19583772};
DE AltName: Full=Antimicrobial peptide H1 {ECO:0000303|PubMed:16269343};
DE Short=Tk-AMP-H1 {ECO:0000303|PubMed:16269343};
DE Contains:
DE RecName: Full=Antimicrobial peptide 1a {ECO:0000303|PubMed:19583772};
DE Short=WAMP-1a {ECO:0000303|PubMed:19583772};
DE Flags: Precursor;
OS Triticum kiharae (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=376535;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Seedling {ECO:0000303|PubMed:22227377};
RX PubMed=22227377; DOI=10.1016/j.biochi.2011.12.023;
RA Andreev Y.A., Korostyleva T.V., Slavokhotova A.A., Rogozhin E.A.,
RA Utkina L.L., Vassilevski A.A., Grishin E.V., Egorov T.A., Odintsova T.I.;
RT "Genes encoding hevein-like defense peptides in wheat: distribution,
RT evolution, and role in stress response.";
RL Biochimie 94:1009-1016(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 35-79, FUNCTION OF ANTIMICROBIAL PEPTIDE 1A, AND MASS
RP SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:19583772};
RX PubMed=19583772; DOI=10.1111/j.1742-4658.2009.07135.x;
RA Odintsova T.I., Vassilevski A.A., Slavokhotova A.A., Musolyamov A.K.,
RA Finkina E.I., Khadeeva N.V., Rogozhin E.A., Korostyleva T.V.,
RA Pukhalsky V.A., Grishin E.V., Egorov T.A.;
RT "A novel antifungal hevein-type peptide from Triticum kiharae seeds with a
RT unique 10-cysteine motif.";
RL FEBS J. 276:4266-4275(2009).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 35-67, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:16269343};
RX PubMed=16269343; DOI=10.1016/j.peptides.2005.03.007;
RA Egorov T.A., Odintsova T.I., Pukhalsky V.A., Grishin E.V.;
RT "Diversity of wheat anti-microbial peptides.";
RL Peptides 26:2064-2073(2005).
RN [4]
RP FUNCTION OF ANTIMICROBIAL PEPTIDE 1B.
RX PubMed=25154438; DOI=10.1111/febs.13015;
RA Slavokhotova A.A., Naumann T.A., Price N.P., Rogozhin E.A., Andreev Y.A.,
RA Vassilevski A.A., Odintsova T.I.;
RT "Novel mode of action of plant defense peptides - hevein-like antimicrobial
RT peptides from wheat inhibit fungal metalloproteases.";
RL FEBS J. 281:4754-4764(2014).
RN [5]
RP STRUCTURE BY NMR OF 35-78, AND DISULFIDE BONDS.
RX PubMed=21704019; DOI=10.1016/j.bbrc.2011.06.058;
RA Dubovskii P.V., Vassilevski A.A., Slavokhotova A.A., Odintsova T.I.,
RA Grishin E.V., Egorov T.A., Arseniev A.S.;
RT "Solution structure of a defense peptide from wheat with a 10-cysteine
RT motif.";
RL Biochem. Biophys. Res. Commun. 411:14-18(2011).
CC -!- FUNCTION: [Antimicrobial peptide 1a]: Binds chitin. Has antifungal
CC activity against the fungi F.solani (IC(50)=5 ug/ml), F.verticillioides
CC (IC(50)=30 ug/ml), F.oxysporum (IC(50)=5 ug/ml), B.sorokiniana
CC (IC(50)=5 ug/ml), B.cinerea (IC(50)=20 ug/ml) and N.crassa (IC(50)=10
CC ug/ml). Inhibits hyphal elongation and causes browning of hyphae in
CC F.oxysporum. Causes destruction and discoloration of spores in
CC B.sorokiniana. Inhibits the development of disease caused by the fungus
CC P.infestans on potato tubers. Has antibacterial activity against the
CC Gram-negative bacteria P.syringae and E.carotovora, and the Gram-
CC positive bacterium C.michiganensis. {ECO:0000269|PubMed:19583772}.
CC -!- FUNCTION: [Antimicrobial peptide 1b]: Has antifungal activity against
CC F.verticillioides (IC(50)=2.7 ug/ml). At concentrations between 45 uM
CC and 225 uM, inhibits activity of metalloproteinase fungalysin Fv-cpm
CC from F.verticillioides. {ECO:0000269|PubMed:25154438}.
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1b]: Mass=4588.1;
CC Method=MALDI; Note=Antimicrobial peptide 1b.;
CC Evidence={ECO:0000269|PubMed:16269343, ECO:0000269|PubMed:19583772};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1a]: Mass=4431.9;
CC Method=MALDI; Note=Antimicrobial peptide 1a.;
CC Evidence={ECO:0000269|PubMed:16269343, ECO:0000269|PubMed:19583772};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1b]: Mass=4590; Method=MALDI;
CC Note=Antimicrobial peptide 1b.; Evidence={ECO:0000269|PubMed:16269343,
CC ECO:0000269|PubMed:19583772};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1a]: Mass=4434; Method=MALDI;
CC Note=Antimicrobial peptide 1a.; Evidence={ECO:0000269|PubMed:16269343,
CC ECO:0000269|PubMed:19583772};
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DR EMBL; HE583764; CCD30733.1; -; mRNA.
DR EMBL; HE583766; CCD30735.1; -; Genomic_DNA.
DR PDB; 2LB7; NMR; -; A=35-78.
DR PDBsum; 2LB7; -.
DR AlphaFoldDB; P85966; -.
DR BMRB; P85966; -.
DR SMR; P85966; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Fungicide; Plant defense;
KW Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:19583772"
FT PEPTIDE 35..79
FT /note="Antimicrobial peptide 1b"
FT /evidence="ECO:0000269|PubMed:19583772"
FT /id="PRO_0000388709"
FT PEPTIDE 35..78
FT /note="Antimicrobial peptide 1a"
FT /evidence="ECO:0000269|PubMed:19583772"
FT /id="PRO_0000388710"
FT PROPEP 80..116
FT /evidence="ECO:0000269|PubMed:19583772"
FT /id="PRO_0000445025"
FT DOMAIN 35..77
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REGION 89..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 38..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:21704019, ECO:0007744|PDB:2LB7"
FT DISULFID 47..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:21704019, ECO:0007744|PDB:2LB7"
FT DISULFID 50..78
FT /evidence="ECO:0000269|PubMed:21704019,
FT ECO:0007744|PDB:2LB7"
FT DISULFID 52..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:21704019, ECO:0007744|PDB:2LB7"
FT DISULFID 71..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:21704019, ECO:0007744|PDB:2LB7"
FT CONFLICT 50
FT /note="C -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2LB7"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2LB7"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2LB7"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2LB7"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2LB7"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2LB7"
SQ SEQUENCE 116 AA; 11460 MW; 32AD96ABEA41F17F CRC64;
MKPHMSATVL RAPRVAAILL AVVLAAVLAT AVNGAQRCGD QARGAKCPNC LCCGKYGFCG
SGDAYCGAGS CQSQCRGCRD DVVGQALPAE PGSTRATAAS SASARGLNLT ATTGGP
