DEFH1_CRAGI
ID DEFH1_CRAGI Reviewed; 60 AA.
AC Q20A06;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Hemocyte defensin Cg-Defh1 {ECO:0000303|PubMed:16962661};
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 {ECO:0000312|EMBL:ABD66301.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 less potent than Cg-Defh2 and Cg-Defm
CC (PubMed:20605792). Shows no or limited activities against Gram-negative
CC bacteria (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 -!- 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=02619";
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DR EMBL; DQ400101; ABD66301.1; -; mRNA.
DR AlphaFoldDB; Q20A06; -.
DR SMR; Q20A06; -.
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-Defh1"
FT /id="PRO_5004199054"
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; 6587 MW; B5867FB8CBD4F730 CRC64;
LFTLVVLLMV SADMAFAGFG CPRDQYKCNS HCQSIGCRAG YCDAVTLWLR CTCTDCNGKK
