ID   AMP_STEME               Reviewed;         478 AA.
AC   U4N938; C0HJD6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Antimicrobial peptide X precursor;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide X;
DE   Flags: Precursor;
GN   Name=sm-amp-x;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 427-459, FUNCTION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, MASS SPECTROMETRY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Seedling;
RX   PubMed=24081691; DOI=10.1007/s11103-013-0127-z;
RA   Slavokhotova A.A., Rogozhin E.A., Musolyamov A.K., Andreev Y.A.,
RA   Oparin P.B., Berkut A.A., Vassilevski A.A., Egorov T.A., Grishin E.V.,
RA   Odintsova T.I.;
RT   "Novel antifungal alpha-hairpinin peptide from Stellaria media seeds:
RT   structure, biosynthesis, gene structure and evolution.";
RL   Plant Mol. Biol. 84:189-202(2014).
CC   -!- FUNCTION: The mature peptide has antifungal activity against germinated
CC       and ungerminated spores of A.alternata (IC(50)=7.4 uM and IC(50)=12.5
CC       uM, respectively), A.niger (IC(50)=2.8 uM and IC(50)=4.0 uM,
CC       respectively), B.cinerea (IC(50)=9.3 uM and IC(50)=16.2 uM,
CC       respectively), F.oxysporum (IC(50)=8.0 uM and IC(50)=5.4 uM,
CC       respectively) and F.solani (IC(50)=8.0 uM and IC(50)=7.2 uM,
CC       respectively). Has no activity against B.sorokiniana, P.infestans and
CC       P.ultimum. Has no antibacterial activity towards C.michiganensis,
CC       E.carotovora, E.coli and P.syringae at concentrations up to 40 uM.
CC       {ECO:0000269|PubMed:24081691}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level). Expressed in
CC       flowers but not in leaves, stem or roots.
CC       {ECO:0000269|PubMed:24081691}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in seedlings and mature plants.
CC       {ECO:0000269|PubMed:24081691}.
CC   -!- DOMAIN: The presence of two CXXXC motifs with connectivity I-IV, II-III
CC       structurally identifies this peptide as an alpha-hairpinin.
CC   -!- MASS SPECTROMETRY: [Antimicrobial peptide X]: Mass=3823.5;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:24081691};
CC   -!- MISCELLANEOUS: Eleven additional peptides containing a similar cysteine
CC       pattern are predicted from this sequence. However, there is only
CC       tentative evidence.
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DR   EMBL; HG423454; CDG56255.1; -; mRNA.
DR   AlphaFoldDB; U4N938; -.
DR   SMR; U4N938; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR006792; Vicilin_N.
DR   Pfam; PF04702; Vicilin_N; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Plant defense; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..478
FT                   /note="Antimicrobial peptide X precursor"
FT                   /id="PRO_0000428653"
FT   PEPTIDE         427..459
FT                   /note="Antimicrobial peptide X"
FT                   /id="PRO_0000428654"
FT   DISULFID        435..455
FT   DISULFID        439..451
SQ   SEQUENCE   478 AA;  55254 MW;  24C835A137A4B43A CRC64;
     MGKLPLLLLL LSVFLTSTLA LRLSNEDRQQ ELGQCLHRCD IRRYSPDMQR ACRHKCHMDF
     GGRKSDEFVV VDYHYEEPEL FSLSPYQMCK FHCRADDSGS FGRMLECEKK CAEEYGNENS
     RNVDERSPSD SRKRFEECRR KCQKTHPDKQ LECIRKCQKA QGERKGDYTF EVCERRCQDT
     RHGSKLACID RCVKEGRDNE GRPVSPKCQK KCEGEGYICQ RMCMKGSDDD TQDRQVSLKC
     QKMCEGKGYD CQKRCMRMDQ SDDNDQDTQV SKMCQKMCQG KSYECQRKCM KECDDDTQGR
     QVSLKCQRMC RGEGYDCQKK CMRIDQSDDN EDPQISKMCQ KMCQGKGYVC ESMCMKGGHD
     DTQCQKMCQG KGDDCQKMCM GMDQSDKNED PQVSQMCQQI CQGEGRGCLQ RCKRAEKVDD
     ANTEMNVDPD VRAYCKHQCM STRGDQARKI CESVCMRQDG KIMLLSTISE VVARLLDD