ID   PEN2A_PENVA             Reviewed;          72 AA.
AC   P81057;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Penaeidin-2a;
DE            Short=P2;
DE            Short=Pen-2;
DE            Short=Pen-2a;
DE   Flags: Precursor;
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-71, FUNCTION, MASS
RP   SPECTROMETRY, AND AMIDATION AT LYS-71.
RC   TISSUE=Hemocyte;
RX   PubMed=9353298; DOI=10.1074/jbc.272.45.28398;
RA   Destoumieux D., Bulet P., Loew D., van Dorsselaer A., Rodriguez J.,
RA   Bachere E.;
RT   "Penaeidins, a new family of antimicrobial peptides isolated from the
RT   shrimp Penaeus vannamei (Decapoda).";
RL   J. Biol. Chem. 272:28398-28406(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-72, PROTEIN SEQUENCE OF 22-71, AND
RP   FUNCTION.
RX   PubMed=10561573; DOI=10.1046/j.1432-1327.1999.00855.x;
RA   Destoumieux D., Bulet P., Strub J.-M., van Dorsselaer A., Bachere E.;
RT   "Recombinant expression and range of activity of penaeidins, antimicrobial
RT   peptides from penaeid shrimp.";
RL   Eur. J. Biochem. 266:335-346(1999).
RN   [3]
RP   CHITIN-BINDING PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Hemocyte;
RX   PubMed=10639333; DOI=10.1242/jcs.113.3.461;
RA   Destoumieux D., Munoz M., Cosseau C., Rodriguez J., Bulet P., Comps M.,
RA   Bachere E.;
RT   "Penaeidins, antimicrobial peptides with chitin-binding activity, are
RT   produced and stored in shrimp granulocytes and released after microbial
RT   challenge.";
RL   J. Cell Sci. 113:461-469(2000).
RN   [4]
RP   REVIEW.
RX   PubMed=11028917; DOI=10.1007/pl00000764;
RA   Destoumieux D., Munoz M., Bulet P., Bachere E.;
RT   "Penaeidins, a family of antimicrobial peptides from penaeid shrimp
RT   (Crustacea, Decapoda).";
RL   Cell. Mol. Life Sci. 57:1260-1271(2000).
CC   -!- FUNCTION: Antibacterial activity against M.luteus and E.coli bacteria.
CC       Antifungal activity against N.crassa and F.oxysporum. Presents chitin-
CC       binding activity. {ECO:0000269|PubMed:10561573,
CC       ECO:0000269|PubMed:9353298}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC       {ECO:0000269|PubMed:10639333}. Note=Cytoplasmic granules of hemocytes
CC       and to a lesser extent in small granules of hemocytes.
CC   -!- TISSUE SPECIFICITY: Higher expression in hemocytes and to a lesser
CC       extent in heart, testis, gills, intestine, lymphoid organ and
CC       hepatopancreas. Traces in eyes and subcuticular epithelium. Not present
CC       in the brain. {ECO:0000269|PubMed:10639333}.
CC   -!- DEVELOPMENTAL STAGE: Expression decreases 3 hours after microbial
CC       challenge to return to control levels after 12 hours and slightly
CC       increases after 24 hours. {ECO:0000269|PubMed:10639333}.
CC   -!- MASS SPECTROMETRY: Mass=5520; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9353298};
CC   -!- SIMILARITY: Belongs to the penaeidin family. {ECO:0000305}.
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DR   EMBL; Y14925; CAA75142.1; -; mRNA.
DR   AlphaFoldDB; P81057; -.
DR   SMR; P81057; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; IPR009226; Penaeidin.
DR   Pfam; PF05927; Penaeidin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..71
FT                   /note="Penaeidin-2a"
FT                   /id="PRO_0000023503"
FT   MOD_RES         71
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:9353298"
FT   DISULFID        45..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..67
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   72 AA;  7833 MW;  5740E69C58673954 CRC64;
     MRLVVCLVFL ASFALVCQGE AYRGGYTGPI PRPPPIGRPP FRPVCNACYR LSVSDARNCC
     IKFGSCCHLV KG