DEFCG_CRAGI
ID DEFCG_CRAGI Reviewed; 65 AA.
AC Q4GWV4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Defensin Cg-Defm {ECO:0000303|PubMed:20605792};
DE AltName: Full=Cg-Def {ECO:0000303|PubMed:16246846};
DE AltName: Full=Mantle defensin {ECO:0000303|PubMed:20605792};
DE Flags: Precursor;
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] {ECO:0007744|PDB:2B68}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], STRUCTURE BY NMR OF 23-65,
RP DISULFIDE BONDS, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Mantle;
RX PubMed=16246846; DOI=10.1074/jbc.m510850200;
RA Gueguen Y., Herpin A., Aumelas A., Garnier J., Fievet J., Escoubas J.M.,
RA Bulet P., Gonzalez M., Lelong C., Favrel P., Bachere E.;
RT "Characterization of a defensin from the oyster Crassostrea gigas.
RT Recombinant production, folding, solution structure, antimicrobial
RT activities, and gene expression.";
RL J. Biol. Chem. 281:313-323(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=20100329; DOI=10.1186/1471-2148-10-23;
RA Schmitt P., Gueguen Y., Desmarais E., Bachere E., de Lorgeril J.;
RT "Molecular diversity of antimicrobial effectors in the oyster Crassostrea
RT gigas.";
RL BMC Evol. Biol. 10:23-23(2010).
RN [3]
RP FUNCTION.
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 (M.lysodeikticus, S.aureus, and the marine bacteria,
CC B.stationis, and M.maritypicum) (PubMed:16246846). It acts by
CC selectively inhibiting peptidoglycan biosynthesis through complex
CC formation with the cell wall precursor lipid II (1:1 molar ratio) thus
CC inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt
CC cell membranes (PubMed:20605792). Is noticeably more potent than Cg-
CC Defh1 (PubMed:20605792). It shows no or limited activities against
CC Gram-negative bacteria and filamentous fungi (PubMed:16246846).
CC {ECO:0000269|PubMed:16246846, ECO:0000269|PubMed:20605792}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000250|UniProtKB:Q53I06}.
CC -!- TISSUE SPECIFICITY: Expressed in the mantle. Low or no expression in
CC most of the organs analyzed, including hemocytes, heart, digestive
CC gland, and gills. {ECO:0000269|PubMed:16246846}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:16246846}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4637.96; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16246846};
CC -!- MISCELLANEOUS: The Cys-26-Pro-27 bond is in cis conformation.
CC {ECO:0000269|PubMed:16246846}.
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=00558";
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DR EMBL; FJ669403; ACQ72990.1; -; Genomic_DNA.
DR EMBL; FJ669404; ACQ72991.1; -; Genomic_DNA.
DR EMBL; FJ669406; ACQ72993.1; -; Genomic_DNA.
DR EMBL; FJ669407; ACQ72994.1; -; Genomic_DNA.
DR EMBL; FJ669409; ACQ72996.1; -; Genomic_DNA.
DR EMBL; FJ669410; ACQ72997.1; -; Genomic_DNA.
DR EMBL; FJ669325; ACQ76260.1; -; mRNA.
DR EMBL; FJ669326; ACQ76261.1; -; mRNA.
DR EMBL; FJ669328; ACQ76263.1; -; mRNA.
DR EMBL; FJ669332; ACQ76267.1; -; mRNA.
DR EMBL; FJ669335; ACQ76270.1; -; mRNA.
DR EMBL; FJ669337; ACQ76272.1; -; mRNA.
DR EMBL; FJ669338; ACQ76273.1; -; mRNA.
DR EMBL; FJ669339; ACQ76274.1; -; mRNA.
DR EMBL; FJ669340; ACQ76275.1; -; mRNA.
DR EMBL; JF766718; AEO44999.1; -; mRNA.
DR EMBL; JF766719; AEO45000.1; -; mRNA.
DR EMBL; JF766720; AEO45001.1; -; mRNA.
DR EMBL; JF766721; AEO45002.1; -; mRNA.
DR EMBL; JF766722; AEO45003.1; -; mRNA.
DR EMBL; JF766732; AEO45013.1; -; mRNA.
DR EMBL; JF766733; AEO45014.1; -; mRNA.
DR EMBL; JF766734; AEO45015.1; -; mRNA.
DR EMBL; JF766735; AEO45016.1; -; mRNA.
DR EMBL; JF766736; AEO45017.1; -; mRNA.
DR EMBL; JF766739; AEO45020.1; -; mRNA.
DR EMBL; JF766741; AEO45022.1; -; mRNA.
DR EMBL; JF766742; AEO45023.1; -; mRNA.
DR EMBL; AM050547; CAJ19280.1; -; Genomic_DNA.
DR EMBL; AJ565499; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 2B68; NMR; -; A=23-65.
DR PDBsum; 2B68; -.
DR AlphaFoldDB; Q4GWV4; -.
DR SMR; Q4GWV4; -.
DR EvolutionaryTrace; Q4GWV4; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Immunity; Innate immunity; Lipid-binding; Membrane; Reference proteome;
KW Secreted; Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..65
FT /note="Defensin Cg-Defm"
FT /evidence="ECO:0000255"
FT /id="PRO_5007703123"
FT REGION 27..30
FT /note="Binds to membrane interface"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT REGION 48..54
FT /note="Binds to membrane interface"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 24
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 25
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 26
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 36
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 56
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 26..47
FT /evidence="ECO:0000269|PubMed:16246846,
FT ECO:0007744|PDB:2B68"
FT DISULFID 33..56
FT /evidence="ECO:0000269|PubMed:16246846,
FT ECO:0007744|PDB:2B68"
FT DISULFID 37..58
FT /evidence="ECO:0000269|PubMed:16246846,
FT ECO:0007744|PDB:2B68"
FT DISULFID 42..61
FT /evidence="ECO:0000269|PubMed:16246846,
FT ECO:0007744|PDB:2B68"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2B68"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2B68"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2B68"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2B68"
SQ SEQUENCE 65 AA; 7008 MW; B1BACAFD2FE7A79A CRC64;
MKVFVLLTLA VLLMVSADMA FAGFGCPGNQ LKCNNHCKSI SCRAGYCDAA TLWLRCTCTD
CNGKK
