PEN3A_PENVA
ID PEN3A_PENVA Reviewed; 82 AA.
AC P81058;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Penaeidin-3a;
DE Short=P3-a;
DE Short=Pen-3a;
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 20-81, PYROGLUTAMATE
RP FORMATION AT GLN-20, FUNCTION, MASS SPECTROMETRY, AND AMIDATION AT SER-81.
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].
RX PubMed=12242595; DOI=10.1007/s00251-002-0487-z;
RA Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S.;
RT "Diversity of the penaeidin antimicrobial peptides in two shrimp species.";
RL Immunogenetics 54:442-445(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-82, PROTEIN SEQUENCE OF 20-31, 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 [4]
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 [5]
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).
RN [6]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=12842879; DOI=10.1074/jbc.m305450200;
RA Yang Y., Poncet J., Garnier J., Zatylny C., Bachere E., Aumelas A.;
RT "Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial
RT peptide.";
RL J. Biol. Chem. 278:36859-36867(2003).
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 -!- PTM: The N-terminus forms pyrrolidone carboxylic acid.
CC {ECO:0000269|PubMed:9353298}.
CC -!- MASS SPECTROMETRY: Mass=6617.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9353298};
CC -!- SIMILARITY: Belongs to the penaeidin family. {ECO:0000305}.
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DR EMBL; Y14926; CAA75143.1; -; mRNA.
DR EMBL; AF387661; AAK73084.1; -; mRNA.
DR EMBL; AF387662; AAK73085.1; -; mRNA.
DR EMBL; AF387663; AAK73086.1; -; mRNA.
DR EMBL; AF390139; AAK77532.1; -; mRNA.
DR PDB; 1UEO; NMR; -; A=20-82.
DR PDBsum; 1UEO; -.
DR AlphaFoldDB; P81058; -.
DR SMR; P81058; -.
DR EvolutionaryTrace; P81058; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:CAFA.
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 3D-structure; Amidation; Antibiotic; Antimicrobial; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Fungicide;
KW Pyrrolidone carboxylic acid; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10561573,
FT ECO:0000269|PubMed:9353298"
FT CHAIN 20..81
FT /note="Penaeidin-3a"
FT /id="PRO_0000023506"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9353298"
FT MOD_RES 81
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:9353298"
FT DISULFID 51..66
FT /evidence="ECO:0000269|PubMed:12842879"
FT DISULFID 55..73
FT /evidence="ECO:0000269|PubMed:12842879"
FT DISULFID 67..74
FT /evidence="ECO:0000269|PubMed:12842879"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1UEO"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1UEO"
SQ SEQUENCE 82 AA; 8748 MW; E60E09BB305521FD CRC64;
MRLVVCLVFL ASFALVCQGQ VYKGGYTRPI PRPPPFVRPL PGGPIGPYNG CPVSCRGISF
SQARSCCSRL GRCCHVGKGY SG
