P25816 (PROF_BETPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Profilin

Alternative name(s):
Allergen Bet v II
Pollen allergen Bet v 2
Allergen=Bet v 2

Gene names

Name:

BETVII

Organism

Betula pendula (European white birch) (Betula verrucosa)

Taxonomic identifier

3505 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fagales › Betulaceae › Betula

Protein attributes

Sequence length	133 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subunit structure	Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Subcellular location	Cytoplasm › cytoskeleton.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the profilin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Disease	Allergen
Ligand	Actin-binding
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 133

132

Profilin

PRO_0000199622

Secondary structure

1

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133

Helix Strand Turn

Details...

Helix

3 – 11

9

Beta strand

24 – 29

6

Beta strand

34 – 37

4

Helix

46 – 57

12

Turn

63 – 65

3

Beta strand

67 – 69

3

Beta strand

72 – 80

9

Turn

81 – 83

3

Beta strand

84 – 89

6

Beta strand

92 – 98

7

Beta strand

100 – 108

9

Helix

114 – 130

17

Sequences

	Sequence		Length	Mass (Da)
	P25816 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 9443FC43786E114A	FASTA	133	14,253
	10 20 30 40 50 60 MSWQTYVDEH LMCDIDGQAS NSLASAIVGH DGSVWAQSSS FPQFKPQEIT GIMKDFEEPG 70 80 90 100 110 120 HLAPTGLHLG GIKYMVIQGE AGAVIRGKKG SGGITIKKTG QALVFGIYEE PVTPGQCNMV 130 VERLGDYLID QGL

References

[1]	"Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals." Valenta R., Duchene M., Pettenburger K., Sillaber C., Valent P., Bettelheim P., Breitenbach M., Rumpold H., Kraft D., Scheiner O. Science 253:557-560(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pollen.
[2]	"The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin." Fedorov A.A., Ball T., Mahoney N.M., Valenta R., Almo S.C. Structure 5:33-45(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[3]	"X-ray crystal structures of birch pollen profilin and Phl p 2." Fedorov A.A., Ball T., Valenta R., Almo S.C. Int. Arch. Allergy Immunol. 113:109-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"Birch pollen profilin: structural organization and interaction with poly-(L-proline) peptides as revealed by NMR." Domke T., Federau T., Schlueter K., Giehl K., Valenta R., Schomburg D., Jockusch B.M. FEBS Lett. 411:291-295(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M65179 mRNA. Translation: AAA16522.1.

PIR

JC2082.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CQA	X-ray	2.40	A	1-133	[»]

ProteinModelPortal

P25816.

SMR

P25816. Positions 2-133.

ModBase

Search...

Protein family/group databases

Allergome

127. Bet v 2.
3136. Bet v 2.0101.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]

PANTHER

PTHR11604. PTHR11604. 1 hit.

Pfam

PF00235. Profilin. 1 hit.
[Graphical view]

PRINTS

PR00392. PROFILIN.
PR01640. PROFILINPLNT.

SMART

SM00392. PROF. 1 hit.
[Graphical view]

SUPFAM

SSF55770. Profilin. 1 hit.

PROSITE

PS00414. PROFILIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25816.

Entry information

Entry name

PROF_BETPN

Accession

Primary (citable) accession number: P25816

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program