DEFH2_CRAGI
ID DEFH2_CRAGI Reviewed; 60 AA.
AC Q20A05;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Hemocyte defensin Cg-Defh2 {ECO:0000303|PubMed:20605792};
DE Flags: Precursor; Fragment;
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY BACTERIA.
RC STRAIN=280406; TISSUE=Hemocyte;
RX PubMed=16962661; DOI=10.1016/j.dci.2006.07.006;
RA Gonzalez M., Gueguen Y., Desserre G., de Lorgeril J., Romestand B.,
RA Bachere E.;
RT "Molecular characterization of two isoforms of defensin from hemocytes of
RT the oyster Crassostrea gigas.";
RL Dev. Comp. Immunol. 31:332-339(2007).
RN [2]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RX PubMed=20605792; DOI=10.1074/jbc.m110.143388;
RA Schmitt P., Wilmes M., Pugniere M., Aumelas A., Bachere E., Sahl H.G.,
RA Schneider T., Destoumieux-Garzon D.;
RT "Insight into invertebrate defensin mechanism of action: oyster defensins
RT inhibit peptidoglycan biosynthesis by binding to lipid II.";
RL J. Biol. Chem. 285:29208-29216(2010).
CC -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive
CC bacteria (PubMed:20605792). It acts by selectively inhibiting
CC peptidoglycan biosynthesis through complex formation with the cell wall
CC precursor lipid II (1:1 molar ratio) thus inhibiting cell wall
CC synthesis (PubMed:20605792). It does not disrupt cell membranes
CC (PubMed:20605792). Is noticeably more potent than Cg-Defh1
CC (PubMed:20605792). {ECO:0000269|PubMed:20605792}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000250|UniProtKB:Q53I06}.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes.
CC {ECO:0000269|PubMed:16962661}.
CC -!- INDUCTION: After a bacterial challenge, the level of transcripts
CC decreases dramatically in the circulating hemocytes. This decrease can
CC be correlated with an increase of transcripts in the gill and the
CC mantle tissue, suggesting a possible migration of the hemocytes
CC expressing Cg-defh2 towards the tissues implicated in the first defense
CC barrier of the oyster. {ECO:0000269|PubMed:16962661}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000250|UniProtKB:Q4GWV4}.
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=02618";
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DR EMBL; DQ400102; ABD66302.1; -; mRNA.
DR AlphaFoldDB; Q20A05; -.
DR SMR; Q20A05; -.
DR Proteomes; UP000005408; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR001542; Defensin_invertebrate/fungal.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR Pfam; PF01097; Defensin_2; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Defensin; Disulfide bond; Immunity;
KW Innate immunity; Lipid-binding; Membrane; Reference proteome; Secreted;
KW Signal; Target cell membrane; Target membrane.
FT SIGNAL <1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..60
FT /note="Hemocyte defensin Cg-Defh2"
FT /id="PRO_5004199107"
FT REGION 22..25
FT /note="Binds to membrane interface"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT REGION 43..49
FT /note="Binds to membrane interface"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 19
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 20
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 21
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 31
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 51
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT DISULFID 21..42
FT /evidence="ECO:0000250|UniProtKB:Q4GWV4"
FT DISULFID 28..51
FT /evidence="ECO:0000250|UniProtKB:Q4GWV4"
FT DISULFID 32..53
FT /evidence="ECO:0000250|UniProtKB:Q4GWV4"
FT DISULFID 37..56
FT /evidence="ECO:0000250|UniProtKB:Q4GWV4"
FT NON_TER 1
FT /evidence="ECO:0000305|PubMed:16962661"
SQ SEQUENCE 60 AA; 6439 MW; C93EC03D2BF29AE2 CRC64;
LLTLAVLLMV SADMAFAGFG CPGDQYECNR HCRSIGCRAG YCDAVTLWLR CTCTGCSGKK
