ID MPAP1_PHLPR Reviewed; 263 AA. AC P43213; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 03-MAY-2023, entry version 121. DE RecName: Full=Pollen allergen Phl p 1; DE AltName: Full=Allergen Phl p I; DE AltName: Allergen=Phl p 1; DE Flags: Precursor; GN Name=PHLPI; OS Phleum pratense (Common timothy). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poodinae; OC Phleinae; Phleum. OX NCBI_TaxID=15957; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN. RC TISSUE=Pollen; RX PubMed=7930302; DOI=10.1016/0091-6749(94)90176-7; RA Laffer S., Valenta R., Vrtala S., Susani M., van Ree R., Kraft D., RA Scheiner O., Duchene M.; RT "Complementary DNA cloning of the major allergen Phl p I from timothy grass RT (Phleum pratense); recombinant Phl p I inhibits IgE binding to group I RT allergens from eight different grass species."; RL J. Allergy Clin. Immunol. 94:689-698(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-263, GLYCOSYLATION AT ASN-32, RP AND SUBUNIT. RX PubMed=9130496; DOI=10.1159/000237520; RA Fedorov A.A., Ball T., Valenta R., Almo S.C.; RT "X-ray crystal structures of birch pollen profilin and Phl p 2."; RL Int. Arch. Allergy Immunol. 113:109-113(1997). CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:9130496}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALLERGEN: Causes an allergic reaction in human. Causes grass pollen CC allergy. Binds to IgE. {ECO:0000269|PubMed:7930302}. CC -!- SIMILARITY: Belongs to the expansin family. Expansin B subfamily. CC {ECO:0000305}. 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; X78813; CAA55390.1; -; mRNA. DR PIR; S44182; S44182. DR PDB; 1N10; X-ray; 2.90 A; A/B=23-263. DR PDBsum; 1N10; -. DR AlphaFoldDB; P43213; -. DR SMR; P43213; -. DR Allergome; 549; Phl p 1. DR Allergome; 551; Phl p 1.0102. DR GlyCosmos; P43213; 1 site, No reported glycans. DR iPTMnet; P43213; -. DR ABCD; P43213; 11 sequenced antibodies. DR EvolutionaryTrace; P43213; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt. DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro. DR CDD; cd22275; DPBB_EXPB_N; 1. DR Gene3D; 2.60.40.760; Expansin, cellulose-binding-like domain; 1. DR Gene3D; 2.40.40.10; RlpA-like domain; 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 PANTHER; PTHR31692:SF21; EXPANSIN-B1; 1. DR PANTHER; PTHR31692; EXPANSIN-B3; 1. 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; SSF50685; Barwin-like endoglucanases; 1. DR SUPFAM; SSF49590; PHL pollen allergen; 1. DR PROSITE; PS50843; EXPANSIN_CBD; 1. DR PROSITE; PS50842; EXPANSIN_EG45; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Disulfide bond; Glycoprotein; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..263 FT /note="Pollen allergen Phl p 1" FT /id="PRO_0000008722" FT DOMAIN 61..167 FT /note="Expansin-like EG45" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DOMAIN 181..262 FT /note="Expansin-like CBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078" FT CARBOHYD 32 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:9130496" FT DISULFID 64..92 FT DISULFID 95..162 FT DISULFID 100..106 FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:1N10" FT TURN 72..76 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:1N10" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:1N10" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 123..131 FT /evidence="ECO:0007829|PDB:1N10" FT HELIX 132..136 FT /evidence="ECO:0007829|PDB:1N10" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:1N10" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 243..250 FT /evidence="ECO:0007829|PDB:1N10" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:1N10" SQ SEQUENCE 263 AA; 28457 MW; 046BA249C17BC048 CRC64; MASSSSVLLV VVLFAVFLGS AYGIPKVPPG PNITATYGDK WLDAKSTWYG KPTGAGPKDN GGACGYKDVD KPPFSGMTGC GNTPIFKSGR GCGSCFEIKC TKPEACSGEP VVVHITDDNE EPIAPYHFDL SGHAFGAMAK KGDEQKLRSA GELELQFRRV KCKYPEGTKV TFHVEKGSNP NYLALLVKYV NGDGDVVAVD IKEKGKDKWI ELKESWGAIW RIDTPDKLTG PFTVRYTTEG GTKTEAEDVI PEGWKADTSY ESK //