EXPB1_MAIZE
ID EXPB1_MAIZE Reviewed; 269 AA.
AC P58738; Q84UA7;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Expansin-B1;
DE AltName: Full=Allergen Zea m 1d;
DE AltName: Full=Beta-expansin-1a;
DE AltName: Full=Pollen allergen Zea m 1;
DE AltName: Full=ZmEXPB1;
DE AltName: Allergen=Zea m 1;
DE Flags: Precursor;
GN Name=EXPB1; Synonyms=EXPB1A;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11351085; DOI=10.1104/pp.126.1.222;
RA Wu Y., Meeley R.B., Cosgrove D.J.;
RT "Analysis and expression of the alpha-expansin and beta-expansin gene
RT families in maize.";
RL Plant Physiol. 126:222-232(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-44, FUNCTION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12913162; DOI=10.1104/pp.103.020024;
RA Li L.-C., Bedinger P.A., Volk C., Jones A.D., Cosgrove D.J.;
RT "Purification and characterization of four beta-expansins (Zea m 1
RT isoforms) from maize pollen.";
RL Plant Physiol. 132:2073-2085(2003).
RN [3]
RP FUNCTION.
RX PubMed=9177257; DOI=10.1073/pnas.94.12.6559;
RA Cosgrove D.J., Bedinger P.A., Durachko D.M.;
RT "Group I allergens of grass pollen as cell wall-loosening agents.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6559-6564(1997).
RN [4]
RP NOMENCLATURE.
RX PubMed=15604683; DOI=10.1007/s11103-004-0158-6;
RA Kende H., Bradford K.J., Brummell D.A., Cho H.-T., Cosgrove D.J.,
RA Fleming A.J., Gehring C., Lee Y., McQueen-Mason S.J., Rose J.K.C.,
RA Voesenek L.A.C.;
RT "Nomenclature for members of the expansin superfamily of genes and
RT proteins.";
RL Plant Mol. Biol. 55:311-314(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 25-269, GLYCOSYLATION AT ASN-34,
RP AND DISULFIDE BONDS.
RX PubMed=16984999; DOI=10.1073/pnas.0605979103;
RA Yennawar N.H., Li L.C., Dudzinski D.M., Tabuchi A., Cosgrove D.J.;
RT "Crystal structure and activities of EXPB1 (Zea m 1), a beta-expansin and
RT group-1 pollen allergen from maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14664-14671(2006).
CC -!- FUNCTION: May aid fertilization by loosening the cell wall of the
CC stigma and style, thereby facilitating penetration of the pollen tube.
CC Acts selectively on grass cell walls, which are relatively poor in
CC pectins and xyloglucans and rich in glucuronoarabinoxylans and (1-
CC 3),(1-4)-beta-D-glucans, when compared with cell walls of other
CC angiosperms, including other monocots. {ECO:0000269|PubMed:12913162,
CC ECO:0000269|PubMed:9177257}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in anthers and pollen.
CC {ECO:0000269|PubMed:12913162}.
CC -!- DEVELOPMENTAL STAGE: Expression low before and high after pollen
CC mitosis.
CC -!- ALLERGEN: Causes an allergic reaction in human. Causes maize pollen
CC allergy.
CC -!- MISCELLANEOUS: Beta-expansin 1 extension activity grass cell wall is
CC enhanced by dithiothreitol (DTT) and EDTA, inhibited by Cu(2+) and
CC Hg(2+), and resistant to denaturation by methanol boiling and heat
CC treatments.
CC -!- SIMILARITY: Belongs to the expansin family. Expansin B subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=EXPANSIN homepage;
CC URL="http://homes.bio.psu.edu/expansins/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF332174; AAK56124.1; -; mRNA.
DR EMBL; AY197353; AAO45608.1; -; mRNA.
DR RefSeq; NP_001288510.1; NM_001301581.1.
DR RefSeq; XP_008659972.1; XM_008661750.1.
DR PDB; 2HCZ; X-ray; 2.75 A; X=25-269.
DR PDBsum; 2HCZ; -.
DR AlphaFoldDB; P58738; -.
DR SMR; P58738; -.
DR STRING; 4577.GRMZM2G146551_P02; -.
DR Allergome; 680; Zea m 1.
DR iPTMnet; P58738; -.
DR PaxDb; P58738; -.
DR PRIDE; P58738; -.
DR EnsemblPlants; Zm00001eb391880_T001; Zm00001eb391880_P001; Zm00001eb391880.
DR GeneID; 103638968; -.
DR GeneID; 103638970; -.
DR Gramene; Zm00001eb391880_T001; Zm00001eb391880_P001; Zm00001eb391880.
DR KEGG; zma:103638968; -.
DR KEGG; zma:103638970; -.
DR MaizeGDB; 403651; -.
DR eggNOG; ENOG502QRTE; Eukaryota.
DR OMA; WRWDGAT; -.
DR OrthoDB; 754048at2759; -.
DR EvolutionaryTrace; P58738; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; P58738; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 2.60.40.760; -; 1.
DR InterPro; IPR007118; Expan_Lol_pI.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR007117; Expansin_CBD.
DR InterPro; IPR036749; Expansin_CBD_sf.
DR InterPro; IPR005795; LolPI.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF03330; DPBB_1; 1.
DR Pfam; PF01357; Expansin_C; 1.
DR PRINTS; PR01225; EXPANSNFAMLY.
DR PRINTS; PR00829; LOLP1ALLERGN.
DR SMART; SM00837; DPBB_1; 1.
DR SUPFAM; SSF49590; SSF49590; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS50843; EXPANSIN_CBD; 1.
DR PROSITE; PS50842; EXPANSIN_EG45; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12913162"
FT CHAIN 25..269
FT /note="Expansin-B1"
FT /id="PRO_0000008724"
FT DOMAIN 63..169
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DOMAIN 183..264
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16984999"
FT DISULFID 66..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079,
FT ECO:0000269|PubMed:16984999"
FT DISULFID 97..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079,
FT ECO:0000269|PubMed:16984999"
FT DISULFID 102..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079,
FT ECO:0000269|PubMed:16984999"
FT CONFLICT 5
FT /note="A -> V (in Ref. 1; AAK56124)"
FT /evidence="ECO:0000305"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2HCZ"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2HCZ"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2HCZ"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2HCZ"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:2HCZ"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:2HCZ"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2HCZ"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2HCZ"
SQ SEQUENCE 269 AA; 29085 MW; 636875ED5C2E02D4 CRC64;
MGSLANNIMV VGAVLAALVA GGSCGPPKVP PGPNITTNYN GKWLTARATW YGQPNGAGAP
DNGGACGIKN VNLPPYSGMT ACGNVPIFKD GKGCGSCYEV RCKEKPECSG NPVTVYITDM
NYEPIAPYHF DLSGKAFGSL AKPGLNDKIR HCGIMDVEFR RVRCKYPAGQ KIVFHIEKGC
NPNYLAVLVK YVADDGDIVL MEIQDKLSAE WKPMKLSWGA IWRMDTAKAL KGPFSIRLTS
ESGKKVIAKD VIPANWRPDA VYTSNVQFY
