MPAP1_PHLPR
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-AUG-2022, entry version 117.
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); Poinae;
OC 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 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 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; 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