BDEF_TACTR
ID BDEF_TACTR Reviewed; 117 AA.
AC P80957;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Big defensin;
DE Flags: Precursor;
OS Tachypleus tridentatus (Japanese horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Tachypleus.
OX NCBI_TaxID=6853;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemocyte;
RX PubMed=9165083; DOI=10.1515/bchm.1997.378.3-4.289;
RA Kawabata S., Saito T., Saeki K., Okino N., Mizutani A., Toh Y., Iwanaga S.;
RT "cDNA cloning, tissue distribution, and subcellular localization of
RT horseshoe crab big defensin.";
RL Biol. Chem. 378:289-292(1997).
RN [2]
RP PROTEIN SEQUENCE OF 39-117, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISULFIDE BONDS.
RC TISSUE=Hemocyte;
RX PubMed=8586631; DOI=10.1093/oxfordjournals.jbchem.a124818;
RA Saito T., Kawabata S., Shingenaga T., Takayenoki Y., Cho J., Nakajima H.,
RA Hirata M., Iwanaga S.;
RT "A novel big defensin identified in horseshoe crab hemocytes: isolation,
RT amino acid sequence, and antibacterial activity.";
RL J. Biochem. 117:1131-1137(1995).
RN [3]
RP PROTEIN SEQUENCE OF 39-72, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph;
RX PubMed=8282718; DOI=10.1093/oxfordjournals.jbchem.a124173;
RA Shigenaga T., Takayenoki Y., Kawasaki S., Seki N., Muta T., Toh Y., Ito A.,
RA Iwanaga S.;
RT "Separation of large and small granules from horseshoe crab (Tachypleus
RT tridentatus) hemocytes and characterization of their components.";
RL J. Biochem. 114:307-316(1993).
RN [4]
RP INTERACTION WITH LICI-1.
RX PubMed=8798603; DOI=10.1074/jbc.271.39.23768;
RA Agarwala K.L., Kawabata S., Miura Y., Kuroki Y., Iwanaga S.;
RT "Limulus intracellular coagulation inhibitor type 3. Purification,
RT characterization, cDNA cloning, and tissue localization.";
RL J. Biol. Chem. 271:23768-23774(1996).
RN [5]
RP STRUCTURE BY NMR OF 39-117.
RX PubMed=18785751; DOI=10.1021/bi800957n;
RA Kouno T., Fujitani N., Mizuguchi M., Osaki T., Nishimura S., Kawabata S.,
RA Aizawa T., Demura M., Nitta K., Kawano K.;
RT "A novel beta-defensin structure: a potential strategy of big defensin for
RT overcoming resistance by Gram-positive bacteria.";
RL Biochemistry 47:10611-10619(2008).
CC -!- FUNCTION: Significantly inhibits the growth of Gram-negative and Gram-
CC positive bacteria and fungi in vitro. {ECO:0000269|PubMed:8586631}.
CC -!- SUBUNIT: Interacts with intracellular coagulation inhibitor 1/LICI-1.
CC {ECO:0000269|PubMed:8798603}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8282718,
CC ECO:0000269|PubMed:8586631, ECO:0000269|PubMed:9165083}. Note=L- and S-
CC granules.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
CC hemocytes, heart, hepatopancreas, stomach, intestine and skeletal
CC muscle. {ECO:0000269|PubMed:8282718, ECO:0000269|PubMed:8586631,
CC ECO:0000269|PubMed:9165083}.
CC -!- SIMILARITY: Belongs to the big defensin family. {ECO:0000305}.
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DR PIR; PC1319; PC1319.
DR PDB; 2RNG; NMR; -; A=39-117.
DR PDB; 2RQ2; NMR; -; A=43-72.
DR PDBsum; 2RNG; -.
DR PDBsum; 2RQ2; -.
DR AlphaFoldDB; P80957; -.
DR BMRB; P80957; -.
DR SMR; P80957; -.
DR TCDB; 1.C.45.5.2; the plant defensin (plant defensin) family.
DR EvolutionaryTrace; P80957; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR Gene3D; 3.40.1620.80; -; 1.
DR InterPro; IPR028060; Defensin_big_dom.
DR InterPro; IPR042033; Defensin_big_N.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR Pfam; PF14862; Defensin_big; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Defensin; Direct protein sequencing;
KW Disulfide bond; Fungicide; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 26..36
FT /id="PRO_0000379923"
FT CHAIN 39..117
FT /note="Big defensin"
FT /id="PRO_0000127109"
FT DISULFID 83..113
FT /evidence="ECO:0000269|PubMed:8586631"
FT DISULFID 90..108
FT /evidence="ECO:0000269|PubMed:8586631"
FT DISULFID 94..114
FT /evidence="ECO:0000269|PubMed:8586631"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:2RNG"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2RNG"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:2RNG"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2RNG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2RNG"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2RNG"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:2RNG"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2RNG"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2RNG"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2RNG"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2RNG"
SQ SEQUENCE 117 AA; 13087 MW; 826DFFB56E200407 CRC64;
MKGNIGIAVF YMLLLLLPTD SIGKKMEEEQ EKLFRQKRNP LIPAIYIGAT VGPSVWAYLV
ALVGAAAVTA ANIRRASSDN HSCAGNRGWC RSKCFRHEYV DTYYSAVCGR YFCCRSR
