CYND4_CYNDA
ID CYND4_CYNDA Reviewed; 522 AA.
AC Q5QJ60;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Berberine bridge enzyme-like Cyn d 4 {ECO:0000305};
DE AltName: Full=60 kDa pollen antigen {ECO:0000303|PubMed:8828524, ECO:0000303|PubMed:8900140};
DE Short=BG60 {ECO:0000303|PubMed:20080962, ECO:0000303|PubMed:8828524, ECO:0000303|PubMed:8900140};
DE AltName: Full=Cyn d BG60 {ECO:0000303|PubMed:20080962};
DE AltName: Full=FAD-linked oxidoreductase BG60 {ECO:0000312|EMBL:AAS02108.1};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Pollen isoallergen BG60 {ECO:0000303|PubMed:10479622, ECO:0000303|PubMed:11162583, ECO:0000303|PubMed:22993084};
DE AltName: Allergen=Cyn d 4 {ECO:0000303|PubMed:22993084};
DE Flags: Precursor;
OS Cynodon dactylon (Bermuda grass) (Panicum dactylon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Chloridoideae; Cynodonteae; Eleusininae; Cynodon.
OX NCBI_TaxID=28909 {ECO:0000312|EMBL:AAS02108.1};
RN [1] {ECO:0000312|EMBL:AAS02108.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chuang J.-G., Chow L.-P., Su S.-N.;
RT "Molecular cloning and expression of an allergen BG60 from Bermuda grass
RT (Cynodon dactylon).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 76-86; 195-218; 347-365 AND 464-476, COFACTOR, TISSUE
RP SPECIFICITY, PTM, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=11162583; DOI=10.1006/bbrc.2000.4203;
RA Liaw S., Lee D.Y., Chow L.P., Lau G.X., Su S.N., Chow L.;
RT "Structural characterization of the 60-kDa bermuda grass pollen
RT isoallergens, a covalent flavoprotein.";
RL Biochem. Biophys. Res. Commun. 280:738-743(2001).
RN [3]
RP TISSUE SPECIFICITY, PTM, GLYCOSYLATION, AND ALLERGEN.
RX PubMed=8828524; DOI=10.1016/s0091-6749(96)70080-5;
RA Su S.N., Shu P., Lau G.X., Yang S.Y., Huang S.W., Lee Y.C.;
RT "Immunologic and physicochemical studies of Bermuda grass pollen antigen
RT BG60.";
RL J. Allergy Clin. Immunol. 98:486-494(1996).
RN [4]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=8900140; DOI=10.1074/jbc.271.43.26653;
RA Ohsuga H., Su S.N., Takahashi N., Yang S.Y., Nakagawa H., Shimada I.,
RA Arata Y., Lee Y.C.;
RT "The carbohydrate moiety of the bermuda grass antigen BG60. New
RT oligosaccharides of plant origin.";
RL J. Biol. Chem. 271:26653-26658(1996).
RN [5]
RP CRYSTALLIZATION, SUBUNIT, TISSUE SPECIFICITY, AND PTM.
RX PubMed=10479622; DOI=10.1006/jsbi.1999.4133;
RA Liaw S.H., Lee D.Y., Yang S.Y., Su S.N.;
RT "Crystallization and preliminary diffraction data of 60-kDa glycosylated
RT pollen isoallergens from Bermuda grass.";
RL J. Struct. Biol. 127:83-87(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, PTM,
RP GLYCOSYLATION, AND ALLERGEN.
RX PubMed=16121337; DOI=10.1002/pmic.200401229;
RA Kao S.H., Su S.N., Huang S.W., Tsai J.J., Chow L.P.;
RT "Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass
RT pollen.";
RL Proteomics 5:3805-3813(2005).
RN [7]
RP ALLERGEN.
RX PubMed=20080962; DOI=10.1074/jbc.m109.058370;
RA Hsu S.C., Chen C.H., Tsai S.H., Kawasaki H., Hung C.H., Chu Y.T.,
RA Chang H.W., Zhou Y., Fu J., Plunkett B., Su S.N., Vieths S., Lee R.T.,
RA Lee Y.C., Huang S.K.;
RT "Functional interaction of common allergens and a C-type lectin receptor,
RT dendritic cell-specific ICAM3-grabbing non-integrin (DC-SIGN), on human
RT dendritic cells.";
RL J. Biol. Chem. 285:7903-7910(2010).
RN [8] {ECO:0007744|PDB:4DNS}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-522 IN COMPLEX WITH FAD,
RP COFACTOR, SUBUNIT, TISSUE SPECIFICITY, DISULFIDE BONDS, AND GLYCOSYLATION
RP AT ASN-88 AND ASN-325.
RX PubMed=22993084; DOI=10.1107/s0907444912027552;
RA Huang T.H., Peng H.J., Su S.N., Liaw S.H.;
RT "Various cross-reactivity of the grass pollen group 4 allergens:
RT crystallographic study of the Bermuda grass isoallergen Cyn d 4.";
RL Acta Crystallogr. D 68:1303-1310(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11162583, ECO:0000269|PubMed:22993084};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:22993084};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10479622,
CC ECO:0000269|PubMed:22993084}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:10479622, ECO:0000269|PubMed:11162583,
CC ECO:0000269|PubMed:16121337, ECO:0000269|PubMed:22993084,
CC ECO:0000269|PubMed:8828524, ECO:0000269|PubMed:8900140}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|PubMed:22993084}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10479622,
CC ECO:0000269|PubMed:11162583, ECO:0000269|PubMed:16121337,
CC ECO:0000269|PubMed:8828524}.
CC -!- PTM: Glycosylated (PubMed:16121337). N-glycosylated (PubMed:8828524,
CC PubMed:8900140). Contains fucose, N-acetylglucosamine, and mannose as
CC main carbohydrates (in a ratio of approximately 3:2:1), and a minute
CC amount of xylose (PubMed:8828524). The two most abundant
CC oligosaccharides are Fuc(1)GlcNAc(2)Man(3) and Fuc(1)GlcNAc(2)Man(2),
CC together comprising about 80% of the total carbohydrate content. They
CC are structurally unusual in having a L-Fuc alpha-(1,3)-linked to Asn-
CC linked GlcNAc without a Xyl beta-(1,2)-linked to the branching Man. The
CC other oligosaccharides make up only 9% of the total carbohydrate
CC content and are characterized by the presence of Xyl beta-(1,2)-linked
CC to the branching Man (PubMed:8900140). {ECO:0000269|PubMed:16121337,
CC ECO:0000269|PubMed:8828524, ECO:0000269|PubMed:8900140}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to Bermuda grass pollen (BGP) (PubMed:8828524,
CC PubMed:16121337). Binds to IgE in all 18 patients tested
CC (PubMed:8828524). Binds to IgE in 50% of the 10 patients tested
CC (PubMed:16121337). Periodate oxidation decreases the binding activity
CC to IgE from 20% to 65% as the concentration of periodate increases from
CC 1 mmol/L to 10 mmol/L, indicating the involvement of the carbohydrate
CC moiety of this protein in immune responses (PubMed:8828524). The
CC fucosylated glycan structures of this protein can bind the human C-type
CC lectin receptors CD209 (DC-SIGN) and its related receptor CLEC4M (L-
CC SIGN). The interaction provokes an immune response leading to the
CC activation of RAF1 and ERK kinases and to the induction of tumor
CC necrosis factor (TNF)-alpha expression in human THP-1 cells and
CC monocyte-derived dendritic cells (MDDCs) (PubMed:20080962).
CC {ECO:0000269|PubMed:16121337, ECO:0000269|PubMed:20080962,
CC ECO:0000269|PubMed:8828524}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AY451241; AAS02108.1; -; mRNA.
DR PDB; 4DNS; X-ray; 2.15 A; A/B=26-522.
DR PDBsum; 4DNS; -.
DR AlphaFoldDB; Q5QJ60; -.
DR SMR; Q5QJ60; -.
DR Allergome; 819; Cyn d 4.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IC:UniProtKB.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Nucleotide-binding; Oxidoreductase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..522
FT /note="Berberine bridge enzyme-like Cyn d 4"
FT /evidence="ECO:0000255"
FT /id="PRO_5004261372"
FT DOMAIN 76..252
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 108..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 176..177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 181..185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT BINDING 461..465
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:22993084, ECO:0007744|PDB:4DNS"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:22993084, ECO:0007744|PDB:4DNS"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 41..98
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT DISULFID 308..329
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT CROSSLNK 113..177
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|PubMed:22993084,
FT ECO:0007744|PDB:4DNS"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4DNS"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4DNS"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:4DNS"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:4DNS"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:4DNS"
FT STRAND 421..430
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 436..449
FT /evidence="ECO:0007829|PDB:4DNS"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4DNS"
FT HELIX 496..506
FT /evidence="ECO:0007829|PDB:4DNS"
SQ SEQUENCE 522 AA; 57413 MW; 3C781F7FC155B33F CRC64;
MARSRAFAFA LLICAVAASC HVALSAPPPY AKQVERDFLT CLTKDIPPRQ LYAKSSPAYA
SVWSSTVRNI KFLSDKTVKP LYIITPTNAS HIQAAVVCGR RHGMRIRVRS GGHDYEGLSY
RSEKPEPFAV VDMNKMRAVS IDGKAATAWV DSGAQLGDLY YGIAKASPKL GFPAGVCTTI
GVGGHFSGGG FGMLLRKYGT AADNVIDAKV VDAQGRLLDR KAMGEDHFWA IRGGGGESFG
IVASWQVKLL PVPPKVTVFQ VHKGIKEGAI DLVTKWQTVA PALPDDLMIR IMAMGQGAMF
EALYLGTCKD LVLLMTARFP ELGMNATHCK EMTWIESVPY IPMGPKGTVR DLLNRTSNIK
AFGKYKSDYV LEPIPKSDWE KIFTWLVKPG AGVMIMDPYG GGIASVPESA TPFPRRSGVL
FNIQYVVYWF GEGAAALPTQ WTRDIYDFMT PYVSKNPRQA YVNYRDLDLG VNQVVGNVST
YASGKVWGEK YFKGNFERLA RTKGKIDPED YFRNEQSIPP LL
