EAP2_EUCUL
ID EAP2_EUCUL Reviewed; 41 AA.
AC P83597;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Antifungal peptide 2;
DE AltName: Full=EAFP2;
OS Eucommia ulmoides (Hardy rubber tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Garryales; Eucommiaceae; Eucommia.
OX NCBI_TaxID=4392;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, DISULFIDE BONDS,
RP AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Bark;
RX PubMed=12067732; DOI=10.1016/s0014-5793(02)02829-6;
RA Huang R.-H., Xiang Y., Liu X.-Z., Zhang Y., Hu Z., Wang D.-C.;
RT "Two novel antifungal peptides distinct with a five-disulfide motif from
RT the bark of Eucommia ulmoides Oliv.";
RL FEBS Lett. 521:87-90(2002).
RN [2]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=15147184; DOI=10.1021/bi036263y;
RA Huang R.H., Xiang Y., Tu G.Z., Zhang Y., Wang D.C.;
RT "Solution structure of Eucommia antifungal peptide: a novel structural
RT model distinct with a five-disulfide motif.";
RL Biochemistry 43:6005-6012(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (0.84 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=15363789; DOI=10.1016/j.jsb.2004.04.002;
RA Xiang Y., Huang R.H., Liu X.Z., Zhang Y., Wang D.C.;
RT "Crystal structure of a novel antifungal protein distinct with five
RT disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution.";
RL J. Struct. Biol. 148:86-97(2004).
CC -!- FUNCTION: Has antifungal activity against P.infestans, A.lycopersici,
CC V.dahliae, G.zeae, A.nicotianae, F.moniliforme, F.oxysporum and
CC C.gossypii. {ECO:0000269|PubMed:12067732}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12067732}.
CC -!- MASS SPECTROMETRY: Mass=4158.91; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12067732};
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DR PDB; 1P9G; X-ray; 0.84 A; A=2-41.
DR PDB; 1P9Z; NMR; -; A=2-41.
DR PDBsum; 1P9G; -.
DR PDBsum; 1P9Z; -.
DR AlphaFoldDB; P83597; -.
DR BMRB; P83597; -.
DR SMR; P83597; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR EvolutionaryTrace; P83597; -.
DR GO; GO:0008061; F:chitin binding; 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; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Fungicide; Plant defense; Pyrrolidone carboxylic acid.
FT CHAIN 1..41
FT /note="Antifungal peptide 2"
FT /id="PRO_0000124817"
FT DOMAIN 4..41
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:12067732"
FT DISULFID 3..17
FT DISULFID 7..37
FT DISULFID 11..23
FT DISULFID 16..30
FT DISULFID 35..39
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1P9G"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1P9Z"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1P9G"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1P9Z"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1P9Z"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1P9G"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1P9G"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1P9G"
SQ SEQUENCE 41 AA; 4186 MW; 8F775334FAABA647 CRC64;
QTCASRCPRP CNAGLCCSIY GYCGSGAAYC GAGNCRCQCR G
