AMP2_STEME
ID AMP2_STEME Reviewed; 163 AA.
AC E1UYU0;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Antimicrobial peptide 2 {ECO:0000305|PubMed:21706181};
DE Short=SmAMP2 {ECO:0000303|PubMed:21706181};
DE Contains:
DE RecName: Full=Antimicrobial peptide 2.1a {ECO:0000305|Ref.2};
DE Short=Sm-AMP-2.1a {ECO:0000303|Ref.2};
DE Contains:
DE RecName: Full=Antimicrobial peptide 2.2a {ECO:0000305|Ref.2};
DE Short=Sm-AMP-2.2a {ECO:0000303|Ref.2};
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:CBJ21249.1};
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 68-99, AND MASS SPECTROMETRY.
RA Vassilevski A.A., Musolyamov A.K., Babakov A.V., Grishin E.V., Egorov T.A.;
RL Submitted (JAN-2010) to UniProtKB.
RN [3] {ECO:0007744|PDB:2N1S}
RP STRUCTURE BY NMR OF 68-97, AND DISULFIDE BONDS.
RA Vassilevski A.A., Bozin T.N., Musolyamov A.K., Panova S.V.,
RA Slavokhotova A.A., Mitkevich V.A., Finkina E.I., Nikonorova A.K.,
RA Ovchinnikova T.V., Arseniev A.S., Babakov A.V., Bocharov E.V.,
RA Grishin E.V., Egorov T.A.;
RT "Common chickweed (Stellaria media) antifungal peptides with chitin-binding
RT domain provide unique plant defense strategy.";
RL Submitted (APR-2015) to the PDB data bank.
CC -!- FUNCTION: [Antimicrobial peptide 2.1a]: Antimicrobial peptide.
CC {ECO:0000250|UniProtKB:E1UYT9}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, stem and leaves.
CC {ECO:0000269|PubMed:21706181}.
CC -!- INDUCTION: Weakly induced (up to 5-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 2.1a]: Mass=3794.5;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 2.1a.;
CC Evidence={ECO:0000269|Ref.2};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2.2a]: Mass=3163.7;
CC Mass_error=0.5; Method=MALDI; Note=Antimicrobial peptide 2.2a.;
CC Evidence={ECO:0000269|Ref.2};
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DR EMBL; FN663152; CBJ21249.1; -; mRNA.
DR PDB; 2N1S; NMR; -; A=68-97.
DR PDBsum; 2N1S; -.
DR AlphaFoldDB; E1UYU0; -.
DR SMR; E1UYU0; -.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; 2.
DR PRINTS; PR00451; CHITINBINDNG.
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; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..57
FT /note="Antimicrobial peptide 2.1a"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000443555"
FT PROPEP 58..67
FT /evidence="ECO:0000305|Ref.2"
FT /id="PRO_0000443556"
FT PEPTIDE 68..99
FT /note="Antimicrobial peptide 2.2a"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000443557"
FT PROPEP 100..163
FT /evidence="ECO:0000305|Ref.2"
FT /id="PRO_0000443558"
FT DOMAIN 26..66
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 69..107
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 DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 41..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 72..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2N1S"
FT DISULFID 77..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2N1S"
FT DISULFID 82..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2N1S"
FT DISULFID 101..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2N1S"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2N1S"
SQ SEQUENCE 163 AA; 17241 MW; 70569BC5F49AA306 CRC64;
MLNMKSFALL MLFATLVGVT IAYDPNGKCG RQYGKCRAGQ CCSQYGYCGS GSKYCAHNTP
LSEIEPTAAG QCYRGRCSGG LCCSKYGYCG SGPAYCGLGM CQGSCLPDMP NHPAQIQART
EAAQAEAQAE AYNQANEAAQ VEAYYQAQTQ AQPQVEPAVT KAP
