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ANN2_AREMA
ID   ANN2_AREMA              Reviewed;         202 AA.
AC   Q5SC59; P84106;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Arenicin-2;
DE   Flags: Precursor;
OS   Arenicola marina (Lugworm) (Lumbricus marinus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Arenicolidae; Arenicola.
OX   NCBI_TaxID=6344;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAV65143.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 182-202, FUNCTION, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Coelomocyte {ECO:0000269|PubMed:15527787};
RX   PubMed=15527787; DOI=10.1016/j.febslet.2004.10.012;
RA   Ovchinnikova T.V., Aleshina G.M., Balandin S.V., Krasnosdembskaya A.D.,
RA   Markelov M.L., Frolova E.I., Leonova Y.F., Tagaev A.A., Krasnodembsky E.G.,
RA   Kokryakov V.N.;
RT   "Purification and primary structure of two isoforms of arenicin, a novel
RT   antimicrobial peptide from marine polychaeta Arenicola marina.";
RL   FEBS Lett. 577:209-214(2004).
RN   [2]
RP   STRUCTURE BY NMR OF 182-202, FUNCTION, AND DISULFIDE BOND.
RX   PubMed=17935487; DOI=10.1042/bj20071051;
RA   Andra J., Jakovkin I., Grotzinger J., Hecht O., Krasnosdembskaya A.D.,
RA   Goldmann T., Gutsmann T., Leippe M.;
RT   "Structure and mode of action of the antimicrobial peptide arenicin.";
RL   Biochem. J. 410:113-122(2008).
CC   -!- FUNCTION: Has antimicrobial activity against the Gram-negative bacteria
CC       E.coli and P.mirabilis, the Gram-positive bacterium L.monocytogenes and
CC       the yeast C.albicans. {ECO:0000269|PubMed:15527787,
CC       ECO:0000269|PubMed:17935487}.
CC   -!- MASS SPECTROMETRY: Mass=2772.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15527787};
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DR   EMBL; AY684857; AAV65143.1; -; mRNA.
DR   PDB; 2JNI; NMR; -; A=182-202.
DR   PDB; 2L8X; NMR; -; A/B=182-202.
DR   PDBsum; 2JNI; -.
DR   PDBsum; 2L8X; -.
DR   AlphaFoldDB; Q5SC59; -.
DR   BMRB; Q5SC59; -.
DR   SMR; Q5SC59; -.
DR   EvolutionaryTrace; Q5SC59; -.
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   InterPro; IPR007084; BRICHOS_dom.
DR   Pfam; PF04089; BRICHOS; 1.
DR   PROSITE; PS50869; BRICHOS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:AAV65143.1"
FT   PROPEP          26..181
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:15527787"
FT                   /id="PRO_0000020733"
FT   PEPTIDE         182..202
FT                   /note="Arenicin-2"
FT                   /evidence="ECO:0000269|PubMed:15527787"
FT                   /id="PRO_0000020734"
FT   DOMAIN          73..168
FT                   /note="BRICHOS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT   DISULFID        100..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..201
FT                   /evidence="ECO:0000269|PubMed:15527787,
FT                   ECO:0000269|PubMed:17935487"
FT   STRAND          184..191
FT                   /evidence="ECO:0007829|PDB:2JNI"
FT   STRAND          194..201
FT                   /evidence="ECO:0007829|PDB:2JNI"
SQ   SEQUENCE   202 AA;  22614 MW;  1C2D0EE65FE75654 CRC64;
     MTSTQSVAVY ATLILAIFCF NDIHCDPIAE ARAAAFGERE ARSAGEWKQF DVNGEKVEVN
     EQENREIIRQ AGGDGVEGSV MVIDHAKGLI IWSIPRAGEC YLIGGVDKQL PDAQELLHYF
     RSAQGSADGE GVQSALDYVK AEDRPVTDLN LLAPEVREAC QGKSVYWLEK SSGDNNEPEK
     RRWCVYAYVR IRGVLVRYRR CW
 
 
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