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EXPB9_MAIZE
ID   EXPB9_MAIZE             Reviewed;         269 AA.
AC   Q07154; Q84UA8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Expansin-B9;
DE   AltName: Full=Beta-expansin-1b;
DE   AltName: Full=Pollen allergen Zea m 1;
DE   AltName: Full=ZmEXPB9;
DE   AltName: Allergen=Zea m 1;
DE   Flags: Precursor;
GN   Name=EXPB9; Synonyms=EXPB1B;
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, AND TISSUE
RP   SPECIFICITY.
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   NUCLEOTIDE SEQUENCE [MRNA] OF 79-269.
RC   TISSUE=Pollen;
RX   PubMed=8406014; DOI=10.1016/0378-1119(93)90297-g;
RA   Broadwater A.H., Rubinstein A.L., Chay C.H., Klapper D.G., Bedinger P.A.;
RT   "Zea mI, the maize homolog of the allergen-encoding Lol pI gene of rye
RT   grass.";
RL   Gene 131:227-230(1993).
RN   [4]
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   [5]
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).
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   -!- 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/";
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DR   EMBL; L14271; AAA33496.1; -; mRNA.
DR   EMBL; AY197352; AAO45607.1; -; mRNA.
DR   PIR; JC1524; JC1524.
DR   RefSeq; NP_001105209.1; NM_001111739.1.
DR   AlphaFoldDB; Q07154; -.
DR   SMR; Q07154; -.
DR   STRING; 4577.GRMZM2G072886_P02; -.
DR   Allergome; 3529; Zea m 1.0101.
DR   Allergome; 680; Zea m 1.
DR   PaxDb; Q07154; -.
DR   PRIDE; Q07154; -.
DR   GeneID; 542106; -.
DR   MaizeGDB; 65840; -.
DR   eggNOG; ENOG502QRTE; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q07154; 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   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-B9"
FT                   /id="PRO_0000154575"
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:0000255"
FT   DISULFID        66..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT   DISULFID        97..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT   DISULFID        102..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
SQ   SEQUENCE   269 AA;  29081 MW;  AFF6F4F72D03B501 CRC64;
     MGSLANNIMV VGAVLAALVV GGSCGPPKVP PGPNITTNYN GKWLTARATW YGQPNGAGAP
     DNGGACGIKN VNLPPYSGMT ACGNVPIFKD GKGCGSCYEV RCKEKPECSG NPVTVFITDM
     NYEPIAPYHF DLSGKAFGSL AKPGLNDKLR HCGIMDVEFR RVRCKYPAGQ KIVFHIEKGC
     NPNYVAVLVK FVADDGDIVL MEIQDKLSAE WKPMKLSWGA IWRMDTAKAL KGPFSIRLTS
     ESGKKVIAKD IIPANWRPDA VYTSNVQFY
 
 
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