ANN1_AREMA
ID ANN1_AREMA Reviewed; 202 AA.
AC Q5SC60; P84105;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Arenicin-1;
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:AAV65142.1}
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=2758.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15527787};
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DR EMBL; AY684856; AAV65142.1; -; mRNA.
DR PDB; 2JSB; NMR; -; A=182-202.
DR PDB; 5M9U; NMR; -; A=182-202.
DR PDBsum; 2JSB; -.
DR PDBsum; 5M9U; -.
DR AlphaFoldDB; Q5SC60; -.
DR BMRB; Q5SC60; -.
DR SMR; Q5SC60; -.
DR TCDB; 1.C.81.1.1; the arenicin (arenicin) family.
DR EvolutionaryTrace; Q5SC60; -.
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"
FT PROPEP 26..181
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15527787"
FT /id="PRO_0000020731"
FT PEPTIDE 182..202
FT /note="Arenicin-1"
FT /evidence="ECO:0000269|PubMed:15527787"
FT /id="PRO_0000020732"
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 183..191
FT /evidence="ECO:0007829|PDB:2JSB"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:2JSB"
SQ SEQUENCE 202 AA; 22497 MW; 2DBA9C9F93F2F430 CRC64;
MTSTQSVAVC ATLILAIFCV NDIHCDPIAE ARAAAFGERE ARSDGEWKQF DVNGEKIEVN
EQENREIIRQ AGGDGVEGSV MVIDHAKGLI SWSIPRAGEC YLIGGVDKQL PDAQELLHYF
QSAQGSADGE GVESALDYVK AEDRPVTDLN LLAPEVREAC QGKSVYWLEK SSGDNNEPEK
RRWCVYAYVR VRGVLVRYRR CW
