AMP_ECHCG
ID AMP_ECHCG Reviewed; 361 AA.
AC B3EWR6; A0A059P9X7; A0A059P9Y0; A0A059P9Y2; A0A059P9Y6; B3EWR4; P86698;
AC V5T948; V5T957; V5T964; V5T971; V5T9J5; V5T9K0; V5T9K7; V5T9L2; V5T9L6;
AC V5T9Z6; V5TA00; V5TA04; V5TA10; V5TA14; V5TAQ1; V5TAQ7; V5TAS1; V5TB77;
AC V5TB82; V5TB87; V5TB92; V5TBA3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Antimicrobial peptides {ECO:0000305|PubMed:21561864};
DE Contains:
DE RecName: Full=Antimicrobial peptide 1 {ECO:0000303|PubMed:21561864};
DE Short=EcAMP1 {ECO:0000303|PubMed:21561864};
DE Contains:
DE RecName: Full=Antimicrobial peptide 3 {ECO:0000303|PubMed:24275143};
DE Short=EcAMP3 {ECO:0000303|PubMed:24275143};
DE Contains:
DE RecName: Full=Antimicrobial peptide 2 {ECO:0000303|PubMed:22940285};
DE Short=EcAMP2 {ECO:0000303|PubMed:22940285};
DE Contains:
DE RecName: Full=Antimicrobial peptide 2.1 {ECO:0000303|PubMed:22940285};
DE Short=EcAMP2.1 {ECO:0000303|PubMed:22940285};
DE Flags: Precursor;
OS Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Boivinellinae; Echinochloa.
OX NCBI_TaxID=90397;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 138-172, FUNCTION
RP (ANTIMICROBIAL PEPTIDE 1 AND ANTIMICROBIAL PEPTIDE 2), AND MASS
RP SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000303|PubMed:24275143}, and
RC Seed {ECO:0000303|PubMed:24275143};
RX PubMed=24275143; DOI=10.1016/j.biochi.2013.11.005;
RA Ryazantsev D.Y., Rogozhin E.A., Dimitrieva T.V., Drobyazina P.E.,
RA Khadeeva N.V., Egorov T.A., Grishin E.V., Zavriev S.K.;
RT "A novel hairpin-like antimicrobial peptide from barnyard grass
RT (Echinochloa crusgalli L.) seeds: Structure-functional and molecular-
RT genetics characterization.";
RL Biochimie 99:63-70(2014).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 92-128, FUNCTION (ANTIMICROBIAL PEPTIDE 1), MASS
RP SPECTROMETRY, DISULFIDE BONDS, AND STRUCTURE BY NMR.
RC TISSUE=Seed {ECO:0000269|PubMed:21561864};
RX PubMed=21561864; DOI=10.1074/jbc.m110.200378;
RA Nolde S.B., Vassilevski A.A., Rogozhin E.A., Barinov N.A., Balashova T.A.,
RA Samsonova O.V., Baranov Y.V., Feofanov A.V., Egorov T.A., Arseniev A.S.,
RA Grishin E.V.;
RT "Disulfide-stabilized helical hairpin structure of a novel antifungal
RT peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).";
RL J. Biol. Chem. 286:25145-25153(2011).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 320-350, FUNCTION (ANTIMICROBIAL PEPTIDE 2 AND
RP ANTIMICROBIAL PEPTIDE 2.1), AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:22940285};
RX PubMed=22940285; DOI=10.1016/j.peptides.2012.08.009;
RA Rogozhin E.A., Ryazantsev D.Y., Grishin E.V., Egorov T.A., Zavriev S.K.;
RT "Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds.";
RL Peptides 38:33-40(2012).
CC -!- FUNCTION: [Antimicrobial peptide 1]: Has antifungal activity. Inhibits
CC spore germination of F.graminearum (EC(50)=4.5 uM), F.oxysporum
CC (EC(50)=8.5 uM), F.solani (EC(50)=4.0 uM), F.verticillioides
CC (EC(50)=8.1 uM), P.infestans (EC(50)=16.3 uM), P.betae (EC(50)=6.0 uM),
CC P.debaryanum (EC(50)=12.0 uM), P.ultimatum (EC(50)=14.4 uM),
CC B.sorokiniana (EC(50)=18.2 uM), A.alternata (EC(50)=16.0 uM) and
CC A.solani (EC(50)=14.0 uM). Does not destroy spores but rather inhibits
CC hyphal growth during germination. Does not affect spore germination in
CC A.niger, C.graminicola, D.maydis and T.album. Does not inhibit trypsin.
CC {ECO:0000269|PubMed:21561864}.
CC -!- FUNCTION: [Antimicrobial peptide 2]: Inhibits spore germination of
CC P.infestans with an IC(50) of 24 uM (PubMed:22940285). EcAMP2 has no
CC activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger
CC at concentration up to 32 uM (PubMed:24275143). Has no antibacterial
CC activity (PubMed:22940285, PubMed:24275143).
CC {ECO:0000269|PubMed:22940285}.
CC -!- FUNCTION: [Antimicrobial peptide 2.1]: Inhibit spore germination of
CC P.infestans with an IC(50) of 24 uM (PubMed:22940285). EcAMP2 has no
CC activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger
CC at concentration up to 32 uM (PubMed:24275143). Has no antibacterial
CC activity (PubMed:22940285, PubMed:24275143).
CC {ECO:0000269|PubMed:22940285}.
CC -!- FUNCTION: [Antimicrobial peptide 3]: Has antifungal activity. Inhibits
CC spore germination of F.graminearum (IC(50)=5.5 uM), F.oxysporum
CC (IC(50)=9.6 uM), B.sorokiniana (IC(50)=15.0 uM) and A.niger
CC (IC(50)=22.4 uM). Has antibacterial activity. Inhibits P.syringae
CC (MIC=4.5 uM), C.michiganensis (MIC=2.1 uM) and E.carotovora (MIC=9.8
CC uM). Does not inhibit trypsin. {ECO:0000269|PubMed:24275143}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28794}.
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 1]: Mass=4271.7;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 1.;
CC Evidence={ECO:0000269|PubMed:21561864};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2]: Mass=3878.8;
CC Method=MALDI; Note=Antimicrobial peptide 2.;
CC Evidence={ECO:0000269|PubMed:22940285};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2.1]: Mass=3333.0;
CC Method=MALDI; Note=Antimicrobial peptide 2.1.;
CC Evidence={ECO:0000269|PubMed:22940285};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 3]: Mass=4428.7;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 3.;
CC Evidence={ECO:0000269|PubMed:24275143};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX875057; AFU90752.1; -; Genomic_DNA.
DR EMBL; JX875059; AFU90754.1; -; Genomic_DNA.
DR EMBL; JX875060; AFU90755.1; -; Genomic_DNA.
DR EMBL; JX875061; AFU90756.1; -; Genomic_DNA.
DR EMBL; KF478770; AHB61267.1; -; Genomic_DNA.
DR EMBL; KF478771; AHB61268.1; -; Genomic_DNA.
DR EMBL; KF478772; AHB61269.1; -; Genomic_DNA.
DR EMBL; KF478773; AHB61270.1; -; Genomic_DNA.
DR EMBL; KF478774; AHB61271.1; -; Genomic_DNA.
DR EMBL; KF478775; AHB61272.1; -; Genomic_DNA.
DR EMBL; KF478776; AHB61273.1; -; Genomic_DNA.
DR EMBL; KF478777; AHB61274.1; -; Genomic_DNA.
DR EMBL; KF478778; AHB61275.1; -; Genomic_DNA.
DR EMBL; KF478779; AHB61276.1; -; Genomic_DNA.
DR EMBL; KF478780; AHB61277.1; -; Genomic_DNA.
DR EMBL; KF478781; AHB61278.1; -; Genomic_DNA.
DR EMBL; KF478782; AHB61279.1; -; Genomic_DNA.
DR EMBL; KF478783; AHB61280.1; -; Genomic_DNA.
DR EMBL; KF478784; AHB61281.1; -; Genomic_DNA.
DR EMBL; KF478785; AHB61282.1; -; Genomic_DNA.
DR EMBL; KF478786; AHB61283.1; -; Genomic_DNA.
DR EMBL; KF478787; AHB61284.1; -; Genomic_DNA.
DR EMBL; KF478788; AHB61285.1; -; Genomic_DNA.
DR EMBL; KF478789; AHB61286.1; -; Genomic_DNA.
DR EMBL; KF478790; AHB61287.1; -; Genomic_DNA.
DR EMBL; KF478791; AHB61288.1; -; Genomic_DNA.
DR EMBL; KF478792; AHB61289.1; -; Genomic_DNA.
DR EMBL; KF478793; AHB61290.1; -; Genomic_DNA.
DR EMBL; KF478794; AHB61291.1; -; Genomic_DNA.
DR EMBL; KF478795; AHB61292.1; -; Genomic_DNA.
DR PDB; 2L2R; NMR; -; A=92-128.
DR PDBsum; 2L2R; -.
DR AlphaFoldDB; B3EWR6; -.
DR BMRB; B3EWR6; -.
DR SMR; B3EWR6; -.
DR PRIDE; B3EWR6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR029227; Plant_Antimicrobial.
DR Pfam; PF14861; Antimicrobial21; 5.
DR SMART; SM01357; Antimicrobial21; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Plant defense; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..361
FT /note="Antimicrobial peptides"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434260"
FT PEPTIDE 92..128
FT /note="Antimicrobial peptide 1"
FT /evidence="ECO:0000269|PubMed:21561864"
FT /id="PRO_0000434261"
FT PEPTIDE 138..172
FT /note="Antimicrobial peptide 3"
FT /evidence="ECO:0000269|PubMed:24275143"
FT /id="PRO_0000434262"
FT PEPTIDE 320..350
FT /note="Antimicrobial peptide 2"
FT /evidence="ECO:0000269|PubMed:22940285"
FT /id="PRO_0000434263"
FT PEPTIDE 320..345
FT /note="Antimicrobial peptide 2.1"
FT /evidence="ECO:0000269|PubMed:22940285"
FT /id="PRO_0000434264"
FT REGION 295..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 98..120
FT /evidence="ECO:0000269|PubMed:21561864"
FT DISULFID 102..116
FT /evidence="ECO:0000269|PubMed:21561864"
FT DISULFID 142..164
FT /evidence="ECO:0000305|PubMed:21561864"
FT DISULFID 146..160
FT /evidence="ECO:0000305|PubMed:21561864"
FT DISULFID 322..342
FT /evidence="ECO:0000305|PubMed:21561864"
FT DISULFID 326..338
FT /evidence="ECO:0000305|PubMed:21561864"
FT CONFLICT 17
FT /note="L -> P (in Ref. 1; AHB61288)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="V -> A (in Ref. 1; AHB61284)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="V -> A (in Ref. 1; AHB61291)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="E -> A (in Ref. 1; AHB61292)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="V -> M (in Ref. 1; AHB61280)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="P -> S (in Ref. 1; AHB61280)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="K -> R (in Ref. 1; AHB61283/AHB61286/AHB61289)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="E -> G (in Ref. 1; AHB61282)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="C -> R (in Ref. 1; AHB61290)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="E -> G (in Ref. 1; AHB61291)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> G (in Ref. 1; AHB61279)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="E -> V (in Ref. 1; AHB61280)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..95
FT /note="EDGSGR -> GRLRQ (in Ref. 1; AHB61269)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..93
FT /note="EDGS -> TAP (in Ref. 1; AHB61268/AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="D -> G (in Ref. 1; AFU90755)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="R -> G (in Ref. 1; AHB61270)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> A (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> G (in Ref. 1; AHB61270)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="C -> R (in Ref. 1; AFU90755)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> G (in Ref. 1; AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> G (in Ref. 1; AHB61271)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="C -> R (in Ref. 1; AHB61268)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> R (in Ref. 1; AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> C (in Ref. 1; AFU90754)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="Missing (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="C -> W (in Ref. 1; AHB61272)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="Missing (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="R -> Q (in Ref. 1; AFU90756)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="T -> A (in Ref. 1; AHB61273)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="R -> G (in Ref. 1; AHB61271)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="C -> Y (in Ref. 1; AHB61272)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> D (in Ref. 1; AFU90752)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> G (in Ref. 1; AFU90755)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> V (in Ref. 1; AHB61268)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="H -> R (in Ref. 1; AHB61272)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="D -> G (in Ref. 1; AHB61276)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> N (in Ref. 1; AFU90756)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> S (in Ref. 1; AHB61276)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> G (in Ref. 1; AHB61269)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="C -> R (in Ref. 1; AHB61273)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="E -> G (in Ref. 1; AHB61270)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="D -> G (in Ref. 1; AHB61269)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> V (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="D -> N (in Ref. 1; AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> N (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="Q -> L (in Ref. 1; AHB61271)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="C -> W (in Ref. 1; AHB61276)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> S (in Ref. 1; AHB61269)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="C -> W (in Ref. 1; AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="P -> S (in Ref. 1; AHB61276)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..313
FT /note="Missing (in Ref. 1; AHB61277/AHB61276/AHB61275/
FT AHB61274/AHB61273/AFU90756)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="D -> N (in Ref. 1; AHB61268)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> G (in Ref. 1; AFU90756)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Q -> R (in Ref. 1; AFU90755/AFU90754/AHB61272/
FT AHB61271/AHB61270/AHB61269/AHB61268/AHB61267/AFU90752)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="Q -> R (in Ref. 1; AFU90756)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="D -> N (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..341
FT /note="MRE -> KRK (in Ref. 1; AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..355
FT /note="RHQGRSDDDDTR -> CHQGRGEDDDTG (in Ref. 1; AHB61276)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..355
FT /note="GRSDDDDTR -> SRGEDDDTG (in Ref. 1; AHB61277)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..355
FT /note="SDDDDTR -> GEDDDTG (in Ref. 1; AHB61275/AHB61274)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> G (in Ref. 1; AHB61272/AHB61271/AHB61270/
FT AHB61269/AHB61268/AHB61267)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="D -> E (in Ref. 1; AHB61273)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..361
FT /note="RAGEDDS -> GAR (in Ref. 1; AHB61269)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..357
FT /note="RAG -> GAD (in Ref. 1; AHB61270)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="R -> G (in Ref. 1; AHB61273/AHB61272/AHB61271/
FT AHB61268/AHB61267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 42048 MW; E3DACDCB17B0F895 CRC64;
MGKGSSGGGA WWAFLLLAGV LLAVAATAAG AEEDVATEVA AAADRDPKED LRWCRKGCQW
QYGQDTRQRK ECERDCRQRH REQEQDADEE DGSGRGSCRS QCMRRHEDEP WRVQECVSQC
RRRRGGGDDD VAVDACEGAD RCRERCERRH RGDWQGKQRC LMECRRREQE EDVDDRCPCP
CRRQCERHGD PATRQRCVEA CQRRREEERR HGGGDADEEG SRGGRCERKC RRHSDWQTRQ
RCLQQCEQRE RQEEGGRDDA GDGKDTYCAD RCQSMCRQRH RGDREMQRRC ARKCEREEGC
PRRRDATADA DEAEEDDGND RCSQQCQHHR DPDRKQQCMR ECRRHQGRSD DDDTRAGEDD
S
