PEN3_PENIN
ID PEN3_PENIN Reviewed; 80 AA.
AC E2IH92;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Penaeidin-3 {ECO:0000303|PubMed:21885268, ECO:0000312|EMBL:ADN43391.1};
DE Short=Fi-Pen3 {ECO:0000303|PubMed:21885268};
DE AltName: Full=Antimicrobial peptide penaeidin 3 {ECO:0000303|PubMed:21885268};
DE Short=AMP penaeidin-3 {ECO:0000303|PubMed:21885268};
DE Flags: Precursor;
GN Name=PEN-3 {ECO:0000312|EMBL:ADN43391.1};
OS Penaeus indicus (Indian white prawn) (Fenneropenaeus indicus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=29960;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, 3D-STRUCTURE MODELING, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Hemocyte {ECO:0000303|PubMed:21885268};
RX PubMed=21885268; DOI=10.1016/j.micres.2011.07.003;
RA Shanthi S., Vaseeharan B.;
RT "cDNA cloning, characterization and expression analysis of a novel
RT antimicrobial peptide gene penaeidin-3 (Fi-Pen3) from the haemocytes of
RT Indian white shrimp Fenneropenaeus indicus.";
RL Microbiol. Res. 167:127-134(2012).
CC -!- FUNCTION: Antibacterial and antifungal activity. Presents chitin-
CC binding activity. {ECO:0000250|UniProtKB:P81058}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of
CC hemocytes and to a lesser extent in small granules of hemocytes.
CC {ECO:0000250|UniProtKB:P81058}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in hemocytes, and to a lesser
CC extent in heart, muscle, gills, intestine and eyestalk. Lowest
CC expression in hepatopancreas. {ECO:0000269|PubMed:21885268}.
CC -!- DEVELOPMENTAL STAGE: Highest expression at premolt stage and lower
CC expression at postmolt and intermolt stages.
CC {ECO:0000269|PubMed:21885268}.
CC -!- INDUCTION: Up-regulated in response to V.parahaemolyticys challenge.
CC Highest expression at 6 hours postinjection of the bacterium, then
CC gradually down-regulated upto 48 hours postinjection.
CC {ECO:0000269|PubMed:21885268}.
CC -!- PTM: The N-terminus forms pyrrolidone carboxylic acid.
CC {ECO:0000250|UniProtKB:P81058}.
CC -!- SIMILARITY: Belongs to the penaeidin family. {ECO:0000305}.
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DR EMBL; HM535650; ADN43391.1; -; mRNA.
DR AlphaFoldDB; E2IH92; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0022404; P:molting cycle process; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR InterPro; IPR009226; Penaeidin.
DR Pfam; PF05927; Penaeidin; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Chitin-binding; Disulfide bond; Fungicide;
KW Pyrrolidone carboxylic acid; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P81058"
FT CHAIN 20..80
FT /note="Penaeidin-3"
FT /evidence="ECO:0000255"
FT /id="PRO_5003159500"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P81058"
FT DISULFID 54..67
FT /evidence="ECO:0000250|UniProtKB:P81058"
FT DISULFID 57..74
FT /evidence="ECO:0000250|UniProtKB:P81058"
FT DISULFID 68..75
FT /evidence="ECO:0000250|UniProtKB:P81058"
SQ SEQUENCE 80 AA; 8483 MW; E567D6CE6D068598 CRC64;
MRLVVCLVYL VSFALVCQGQ GFKGGYTGSY SRAPPYGSRG PISTHPISRP ATGCTSCHTI
TFDKAACCRL FGRCCSALKG
