MPA5B_PHLPR
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 25-MAY-2022, entry version 85.
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); Poinae;
OC 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}.
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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:ribonuclease activity; IDA:CACAO.
DR Gene3D; 1.20.120.320; -; 2.
DR InterPro; IPR002914; Poa_pIX/Phl_pVI.
DR InterPro; IPR035506; Pollen_allergen/Os.
DR Pfam; PF01620; Pollen_allerg_2; 2.
DR SUPFAM; SSF81736; SSF81736; 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