GNK2_GINBI
ID GNK2_GINBI Reviewed; 134 AA.
AC A4ZDL6; C3VHZ7; F2Q6K2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Antifungal protein ginkbilobin-2 {ECO:0000303|PubMed:17338634};
DE AltName: Full=Antimicrobial protein Gnk2-1 {ECO:0000312|EMBL:ACP27608.1};
DE Flags: Precursor;
GN Name=GNK2 {ECO:0000305}; Synonyms=GNK2-1 {ECO:0000312|EMBL:ACP27608.1};
OS Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX NCBI_TaxID=3311;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-56, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Seed;
RX PubMed=17338634; DOI=10.1515/bc.2007.030;
RA Sawano Y., Miyakawa T., Yamazaki H., Tanokura M., Hatano K.;
RT "Purification, characterization, and molecular gene cloning of an
RT antifungal protein from Ginkgo biloba seeds.";
RL Biol. Chem. 388:273-280(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Seed {ECO:0000312|EMBL:ACP27608.1};
RA Liu J., Wang Y.H., Wang Q., Tian H.L., Guo A.G.;
RT "Isolation and functional characterization of Ginkgo biloba antimicrobial
RT protein gene and its promoter.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
RX PubMed=26315821; DOI=10.1007/s00709-015-0876-4;
RA Gao N., Wadhwani P., Muehlhaeuser P., Liu Q., Riemann M., Ulrich A.S.,
RA Nick P.;
RT "An antifungal protein from Ginkgo biloba binds actin and can trigger cell
RT death.";
RL Protoplasma 253:1159-1174(2016).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 27-134.
RX PubMed=17768341; DOI=10.1107/s1744309107034793;
RA Miyakawa T., Sawano Y., Miyazono K., Hatano K., Tanokura M.;
RT "Crystallization and preliminary X-ray analysis of ginkbilobin-2 from
RT Ginkgo biloba seeds: a novel antifungal protein with homology to the
RT extracellular domain of plant cysteine-rich receptor-like kinases.";
RL Acta Crystallogr. F 63:737-739(2007).
RN [5]
RP ERRATUM OF PUBMED:17768341.
RA Miyakawa T., Sawano Y., Miyazono K., Hatano K., Tanokura M.;
RL Acta Crystallogr. F 63:899-899(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 27-134, AND DISULFIDE BONDS.
RX PubMed=19603485; DOI=10.1002/prot.22494;
RA Miyakawa T., Miyazono K., Sawano Y., Hatano K., Tanokura M.;
RT "Crystal structure of ginkbilobin-2 with homology to the extracellular
RT domain of plant cysteine-rich receptor-like kinases.";
RL Proteins 77:247-251(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 27-134 IN COMPLEX WITH MANNOSE,
RP FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF ARG-119.
RX PubMed=25139159; DOI=10.1104/pp.114.242636;
RA Miyakawa T., Hatano K., Miyauchi Y., Suwa Y., Sawano Y., Tanokura M.;
RT "A secreted protein with plant-specific cysteine-rich motif functions as a
RT mannose-binding lectin that exhibits antifungal activity.";
RL Plant Physiol. 166:766-778(2014).
RN [8]
RP ERRATUM OF PUBMED:25139159.
RX PubMed=25725072; DOI=10.1104/pp.115.900504;
RA Miyakawa T., Hatano K., Miyauchi Y., Suwa Y., Sawano Y., Tanokura M.;
RL Plant Physiol. 167:1204-1204(2015).
CC -!- FUNCTION: Possesses antifungal activity against F.oxysporum, T.reesei
CC and C.albicans. Weakly inhibits the aspartic acid protease pepsin
CC activity (PubMed:17338634). Exerts antifungal activity against
CC S.cerevisiae and F.culmorum through its carbohydrate-binding
CC specificity. Acts as a lectin that stricly recognizes alpha-1,2-linked
CC mannose moieties and interacts with the yeast cell wall mannan
CC polysaccharide (PubMed:25139159). Can interfere with the fungal actin
CC remodeling resulting to the activation of an actin-dependent cell death
CC (PubMed:26315821). {ECO:0000269|PubMed:17338634,
CC ECO:0000269|PubMed:25139159, ECO:0000269|PubMed:26315821}.
CC -!- SUBUNIT: Binds actin in vitro. {ECO:0000269|PubMed:26315821}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26315821}.
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DR EMBL; DQ496113; ABF55255.1; -; mRNA.
DR EMBL; FJ822053; ACZ57929.1; -; Genomic_DNA.
DR EMBL; FJ865399; ACP27608.1; -; mRNA.
DR PDB; 3A2E; X-ray; 2.38 A; A/B/C/D=27-134.
DR PDB; 4XRE; X-ray; 2.60 A; A/B/C/D=27-134.
DR PDBsum; 3A2E; -.
DR PDBsum; 4XRE; -.
DR AlphaFoldDB; A4ZDL6; -.
DR BMRB; A4ZDL6; -.
DR SMR; A4ZDL6; -.
DR UniLectin; A4ZDL6; -.
DR EvolutionaryTrace; A4ZDL6; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0012502; P:induction of programmed cell death; NAS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.430.20; -; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR Pfam; PF01657; Stress-antifung; 1.
DR PROSITE; PS51473; GNK2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Antibiotic; Antimicrobial; Apoptosis;
KW Direct protein sequencing; Disulfide bond; Fungicide; Lectin;
KW Mannose-binding; Plant defense; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..134
FT /note="Antifungal protein ginkbilobin-2"
FT /id="PRO_5000242182"
FT DOMAIN 29..134
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT BINDING 37
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0007744|PDB:4XRE"
FT BINDING 119
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0007744|PDB:4XRE"
FT BINDING 130
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0007744|PDB:4XRE"
FT DISULFID 36..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806,
FT ECO:0000269|PubMed:19603485, ECO:0007744|PDB:3A2E,
FT ECO:0007744|PDB:4XRE"
FT DISULFID 88..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806,
FT ECO:0000269|PubMed:19603485, ECO:0007744|PDB:3A2E,
FT ECO:0007744|PDB:4XRE"
FT DISULFID 100..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806,
FT ECO:0000269|PubMed:19603485, ECO:0007744|PDB:3A2E,
FT ECO:0007744|PDB:4XRE"
FT MUTAGEN 119
FT /note="R->A: Abolishes binding to yeast mannan."
FT /evidence="ECO:0000269|PubMed:25139159"
FT CONFLICT 30
FT /note="A -> N (in Ref. 2; ACP27608)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="R -> K (in Ref. 2; ACP27608)"
FT /evidence="ECO:0000305"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3A2E"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3A2E"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:3A2E"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3A2E"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3A2E"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3A2E"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:3A2E"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3A2E"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:3A2E"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:3A2E"
SQ SEQUENCE 134 AA; 14473 MW; A690A49536F44CFE CRC64;
MKTMRMNSAF ILAFALAAAM LILTEAANTA FVSSACNTQK IPSGSPFNRN LRAMLADLRQ
NTAFSGYDYK TSRAGSGGAP TAYGRATCKQ SISQSDCTAC LSNLVNRIFS ICNNAIGARV
QLVDCFIQYE QRSF
