ID MPA5B_PHLPR Reviewed; 284 AA. AC Q40963; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 28-JUN-2023, entry version 90. DE RecName: Full=Pollen allergen Phl p 5b; DE AltName: Full=Allergen Phl p Vb; DE AltName: Allergen=Phl p 5b; DE Flags: Precursor; Fragment; 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]. RC STRAIN=Agrostideae; TISSUE=Pollen; RX PubMed=7729555; DOI=10.1016/0014-5793(95)00259-c; RA Bufe A., Schramm G., Keown M.B., Schlaak M., Becker W.M.; RT "Major allergen Phl p Vb in timothy grass is a novel pollen RNase."; RL FEBS Lett. 363:6-12(1995). RN [2] RP SEQUENCE REVISION. RA Bufe A.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 150-251, SUBUNIT, AND DISULFIDE RP BOND. RX PubMed=12077438; DOI=10.1107/s0907444902007254; RA Rajashankar K., Bufe A., Weber W., Eschenburg S., Lindner B., Betzel C.; RT "Structure of the functional domain of the major grass-pollen allergen Phlp RT 5b."; RL Acta Crystallogr. D 58:1175-1181(2002). CC -!- FUNCTION: Has ribonuclease activity. May be involved in host-pathogen CC interactions. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12077438}. CC -!- ALLERGEN: Causes an allergic reaction in human. Causes grass pollen CC allergy. CC -!- SIMILARITY: Belongs to the Poa p IX/Phl p VI allergen family. 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; Z27083; CAA81609.1; -; mRNA. DR PDB; 1L3P; X-ray; 1.98 A; A=150-251. DR PDBsum; 1L3P; -. DR AlphaFoldDB; Q40963; -. DR SMR; Q40963; -. DR Allergome; 558; Phl p 5. DR Allergome; 567; Phl p 5.0201. DR EvolutionaryTrace; Q40963; -. DR GO; GO:0004540; F:RNA nuclease activity; IDA:CACAO. DR CDD; cd12805; Allergen_V_VI; 1. DR Gene3D; 1.20.120.320; Group V grass pollen allergen; 2. DR InterPro; IPR002914; Poa_pIX/Phl_pVI. DR InterPro; IPR035506; Pollen_allergen/Os. DR Pfam; PF01620; Pollen_allerg_2; 2. DR PRINTS; PR00833; POAALLERGEN. DR SUPFAM; SSF81736; Group V grass pollen allergen; 2. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Disulfide bond; Signal. FT SIGNAL <1..19 FT /evidence="ECO:0000255" FT CHAIN 20..284 FT /note="Pollen allergen Phl p 5b" FT /id="PRO_0000021746" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 205 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:12077438" FT NON_TER 1 FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 158..173 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 180..195 FT /evidence="ECO:0007829|PDB:1L3P" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 207..218 FT /evidence="ECO:0007829|PDB:1L3P" FT TURN 219..222 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1L3P" FT HELIX 228..250 FT /evidence="ECO:0007829|PDB:1L3P" SQ SEQUENCE 284 AA; 28002 MW; E949FB3E0985295E CRC64; AAAAVPRRGP RGGPGRSYTA DAGYAPATPA AAGAAAGKAT TEEQKLIEDI NVGFKAAVAA AASVPAADKF KTFEAAFTSS SKAAAAKAPG LVPKLDAAYS VAYKAAVGAT PEAKFDSFVA SLTEALRVIA GALEVHAVKP VTEEPGMAKI PAGELQIIDK IDAAFKVAAT AAATAPADDK FTVFEAAFNK AIKESTGGAY DTYKCIPSLE AAVKQAYAAT VAAAPQVKYA VFEAALTKAI TAMSEVQKVS QPATGAATVA AGAATTAAGA ASGAATVAAG GYKV //